CN111247165A - 人血清白蛋白变体及其应用 - Google Patents
人血清白蛋白变体及其应用 Download PDFInfo
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Abstract
血清白蛋白变体或其功能片段，其包含选自下述的一个或多个氨基酸取代：(i)甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸取代位置(522)处的谷氨酰胺；(ii)缬氨酸取代位置(552)处的丙氨酸；和(iii)丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸取代位置(572)处的甘氨酸。
Description
相关申请信息
本申请要求2017年10月18日提交的题为“人血清白蛋白变体及其应用”的澳大利亚专利申请号2017904211的优先权。其全部内容通过引用并入本文。
序列表
本申请与电子格式的序列表一同提交。该序列表的全部内容通过引用纳入本文。
技术领域
本公开涉及人血清白蛋白变体及其应用。
背景
血清白蛋白是人血浆中最丰富的天然蛋白质，并在维持血液的渗透压以及在血液中运输各种物质中起着重要作用。
已知血清白蛋白在体内结合多种蛋白质，包括新生Fc受体(FcRn)，并且已知这种相互作用对于白蛋白的血浆半衰期十分重要。FcRn是一种膜结合蛋白，在许多细胞和组织类型(例如，内皮细胞)中表达，并且不断被内化和回收。白蛋白在中性pH下不结合FcRn，但是内吞的白蛋白在核内体的酸性条件下结合FcRn。由降解中解救FcRN结合的白蛋白，并与FcRn一起回收回到细胞表面，在那里，在生理pH下，它与FcRn解离。
白蛋白具有大约19天的长血浆半衰期。该长半衰期导致使用白蛋白来延长药物化合物的半衰期。例如，白蛋白已与人凝血因子IX(FIX)融合在一起，从而延长了FIX
的半衰期。白蛋白还已经与化疗化合物(如紫杉醇)偶联，以增加药物的半衰期和药物积累(例如，
)。
先前已经描述了这样的人血清白蛋白变体，相较于天然血清白蛋白，其具有导致与FcRn的结合或对FcRn的亲和力改善的一个或多个氨基酸取代(例如，WO2011051489)。
然而，本领域技术人员清楚的是，本领域持续需要具有改善的药代动力学性质(如对FcRn的亲和力增加，血浆半衰期增加和/或清除降低)的血清白蛋白变体。本领域中还需要开发用于控制血浆中药物血浆半衰期以优化药物剂量和累积的方法。
发明内容
本公开基于发明人这样的发现，即血清白蛋白中的某些氨基酸取代改善或增加了其与新生Fc受体(FcRn)的结合。具有某些氨基酸取代的血清白蛋白变体能够延长血浆半衰期。
发明人已经确定，SEQ ID NO:1的残基522、552和572对与FcRn的结合十分重要。此外，发明人已经发现，在某些残基处用某些氨基酸取代可以增加或增强酸性pH下与FcRn的结合。
发明人的发现为这样的血清白蛋白变体提供了基础，所述血清白蛋白变体在对应SEQ ID NO：1氨基酸522、552或572的残基处包含一个或多个氨基酸取代。发明人的发现还为这样的方法提供了基础，所述方法用于治疗疾病，例如对象中的出血疾病。
本公开提供了血清白蛋白变体或其功能片段，其包含选自下组的一种或多种氨基酸取代：
(i).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸；
(ii).缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸；
(iii).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸；和
(iv).其组合。
在一个实例中，血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含甘氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含异亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含赖氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含甲硫氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含苯丙氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含色氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含酪氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含缬氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含丙氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的谷氨酰胺。
在一个实例中，血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含丙氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含谷氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含组氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含丝氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含赖氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含缬氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含如上所示对应SEQ ID NO:1氨基酸522、SEQ ID NO:1氨基酸552和SEQ ID NO:1氨基酸572的位置处的氨基酸取代。
在一个实例中，血清白蛋白变体或其功能片段，除了如上所示对应SEQ ID NO:1氨基酸522、SEQ ID NO:1氨基酸552和SEQ ID NO:1氨基酸572的位置处的氨基酸取代以外，任选地包含一个或多个氨基酸取、缺失或插入。适用于本公开的其他氨基酸取代对于本领域技术人员而言是显而易见的并且包括天然产生的取代以及工程改造的取代，例如，WO2011051489中所述的那些。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，本公开的血清白蛋白变体或其功能片段的药代动力学改善。血清白蛋白的药代动力学对于本领域技术人员而言是显而易见的并且包括例如，与FcRn的结合亲和力，血浆半衰期和/或血浆清除率。用于确定本公开的血清白蛋白变体的药代动力学的方法对于本领域技术人员而言将是显而易见的和/或述于本文。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，本公开的血清白蛋白变体或其功能片段对FcRn结合的亲和力增加。用于确定血清白蛋白变体或其功能片段对FcRn的亲和力的方法对于本领域技术人员而言将是显而易见的和/或述于本文。在一个实例中，血清白蛋白或其功能片段对FcRn的结合亲和力通过流式细胞术确定。例如，稳定表达血清白蛋白变体或其功能片段的CHO细胞在酸性(pH 5.5)和中性(pH 7.4)pH下用alexa-488标记的FcRn/β2m(检测靶标结合)和抗myc-alexa 647(检测表达)染色，并通过流式细胞术进行分析。在一个实例中，血清白蛋白变体或其功能片段对FcRn/β2m的亲和力通过计算相对于未修饰的血清白蛋白(例如，如SEQ ID NO:1所示)的平均荧光强度来确定。在一个实例中，血清白蛋白或其功能片段亲和力通过生物传感器分析(例如，使用表面等离子体共振(SPR)试验)来确定。例如，血清白蛋白变体或其功能片段与固定的FcRn的结合亲和力(即，相互作用的强度)在pH 5.4和/或pH 7.4、37℃确定。例如，固定的血清白蛋白变体或其功能片段与FcRn的结合亲和力(即，相互作用的强度)在pH 5.4和/或pH 7.4、37℃确定。在一个实例中，确定亲和力常数(KD)、解离常数(Kd)和结合常数(Ka)。例如，亲和力常数(KD)是解离常数(Kd)和结合常数(Ka)的比例(即，KD＝Kd/Ka)。
在一个实例中，结合亲和力在酸性pH下测量。例如，酸性pH是小于约pH 6.0的pH，如约pH 5.9、或约pH 5.8、或约pH 5.7、或约pH 5.6、或约pH 5.5、或约pH 5.4、或约pH 5.3、或约pH 5.2、或约pH 5.1、或约pH 5.0。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，本公开的血清白蛋白变体或其功能片段在酸性pH下对FcRn结合的亲和力增加。在一个实例中，在较低的pH，例如，约pH 6.0下，本公开的血清白蛋白变体或其功能片段对FcRn结合的亲和力增加，以促进核内体中的结合。在一个实例中，相较于血清白蛋白变体或其功能片段在pH 7.4下的亲和力，血清白蛋白变体或其功能片段在约pH 6.0下对FcRn结合的亲和力增加，这促进了细胞回收后血清白蛋白变体重新释放到血液中。本公开的氨基酸取代通过增加FcRn介导的回收并由此减少由血液清除能够用于延长蛋白质的半衰期。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，通过细胞结合研究确定，本公开的血清白蛋白变体或其功能片段在pH 5.4下对FcRn的结合水平增加。在一个实例中，相较于其在pH 7.4下的亲和力，通过细胞结合研究确定，本公开的血清白蛋白变体或其功能片段在pH 5.4下对FcRn结合水平增加。在一个实例中，相较于其在pH 7.4下的亲和力，通过SPR分析确定，本公开的血清白蛋白变体或其功能片段在pH 5.4下对FcRn结合水平增加。在一个实例中，相较于其在pH 7.4下的亲和力，通过流式细胞术确定，本公开的血清白蛋白变体或其功能片段在pH 5.4下对FcRn结合水平增加。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，本公开的血清白蛋白变体或其功能片段对FcRn的结合水平增加至少约2倍数、或至少约4倍、或至少约5倍、或至少约10倍、或至少约15倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，本公开的血清白蛋白变体对FcRn的结合水平增加约2倍至约5倍。例如，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约2倍、或约2.25倍、或约2.5倍、或约2.75倍、或约3倍、或约3.25倍、或约3.5倍、或约3.75倍、或约4倍、或约4.25倍、或约4.5倍、或约4.75倍、或约5倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约2.4倍、或约2.8倍、或约3.1倍、或约3.4倍、或约3.7倍、或约3.9倍、或约4倍、或约4.8倍。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约5倍至约15倍。在一个实例中，血清白蛋白变体对FcRn的结合水平增加约5倍、或约5.5倍、或约6倍、或约6.5倍、或约7倍、或约7.5倍、或约8倍、或约8.5倍、或约9倍、或约9.5倍、或约10倍、或约10.5倍、或约11倍、或约11.5倍、或约12倍、或约12.5倍、或约13倍、或约13.5倍、或约14倍、或约14.5倍、或约15倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约7.6倍、或约8.6倍、或约13.8倍。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约15倍至约50倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约15倍、或约20倍、或约25倍、或约30倍、或约35倍、或约40倍、或约45倍、或约50倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约42倍、或约43倍、或约47倍、或约48倍。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约50倍至约100倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约50倍、或约55倍、或约60倍、或约65倍、或约70倍、或约75倍、或约80倍、或约85倍、或约90倍、或约95倍、或约100倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约57倍或约58倍。
在另一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约100倍至约250倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约100倍、或约110倍、或约120倍、或约130倍、或约140倍、或约150倍、或约160倍、或约170倍、或约180倍、或约190倍、或约200倍、或约210倍、或约220倍、或约230倍、或约240倍、或约250倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约180倍或约240倍。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加至少约250倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约200倍、或约250倍、或约300倍、或约350倍、或约400倍、或约450倍、或约500倍。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体对FcRn的结合水平增加约410倍。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体的血清半衰期增加。例如，相较于SEQ ID NO:1中所示的血清白蛋白，本公开的血清白蛋白变体的血清半衰期增加至少约1.5倍。在一个实例中，本公开的血清白蛋白变体的血清半衰期增加约1.5倍、或约2倍、或约2.5倍、或约3倍、或约3.5倍、或约4倍、或约4.5倍、或约5倍、或约5.5倍、或约6倍、或约6.5倍、或约7倍、或约7.5倍、或约8倍、或约8.5倍、或约9倍、或约9.5倍、或约10倍。在一个实例中，本公开的血清白蛋白变体的血清半衰期增加约5天至约10天或更多天。例如，本公开的血清白蛋白变体的血清半衰期增加约5天、或约6天、或约7天、或约8天、或约9天、或约10天、或约11天、或约12天、或约13天、或约14天、或约15天、或约16天、或约17天、或约18天、或约19天、或约20天、或约25天、或约30天、或约35天、或约40天、或约45天、或约50天。用于确定血清白蛋白变体的半衰期的方法对于本领域技术人员而言将是显而易见的和/或述于本文。在一个实例中，使用体内试验确定血清白蛋白变体的半衰期。在一个实例中，使用人血清白蛋白特异性抗体在酶联免疫吸附测定(ELISA)中测量血清白蛋白浓度。例如，使用市售可得的方法进行ELISA。在另一个实例中，将血清白蛋白变体静脉内注射到小鼠或食蟹猴中，并随时间定期测量血浆浓度。在一个实例中，在注射后3分钟至72小时测量血清白蛋白变体的血浆浓度。在一个实例中，在注射后直至60天测量血清白蛋白变体的血浆浓度。在一个实例中，放射性标记血清白蛋白变体。在一个实例中，通过计算β相的清除率来确定血清白蛋白变体或其功能片段的体内半衰期。在一个实例中，血清白蛋白变体或其功能片段的体内半衰期与未修饰的血清白蛋白(例如，如SEQ ID NO:1所示)的体内半衰期比较。
在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，血清白蛋白变体清除的速率(即，回收和摄取)降低。用于确定血清白蛋白变体清除速率(例如，回收和摄取)的方法对于本领域技术人员而言将是显而易见的和/或述于本文。在一实施例中，使用共聚焦荧光显微镜确定血清白蛋白变体是否被回收。例如，为了确定血清白蛋白变体是否被回收，将荧光标记的血清白蛋白变体与在细胞表面上表达人FcRn受体的细胞一起孵育并通过共聚焦荧光显微镜观察。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含：
(i).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，和缬氨酸取代SEQ ID NO:1位置552处的丙氨酸；或
(ii).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，和选自下组的氨基酸取代SEQ ID NO:1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸；或
(iii).缬氨酸取代对应SEQ ID NO：1氨基酸552的位置处的丙氨酸，和选自下组的氨基酸取代位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸；或
(iv).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，缬氨酸取代SEQ ID NO:1位置572处的丙氨酸，和选自下组的氨基酸取代SEQ ID NO:1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，和缬氨酸取代SEQ ID NO:1位置552处的丙氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，和选自下组的氨基酸取代SEQ ID NO:1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含缬氨酸取代对应SEQID NO：1氨基酸552的位置处的丙氨酸，和选自下组的氨基酸取代SEQ ID NO：1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，缬氨酸取代SEQ ID NO:1位置572处的丙氨酸，和选自下组的氨基酸取代SEQ ID NO:1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段还包含酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，血清白蛋白变体或其功能片段包含缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，缬氨酸取代SEQ ID NO:1位置552处的丙氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，选自下组的氨基酸取代SEQ ID NO:1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸，和酪氨酸取代对应SEQ IDNO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含缬氨酸取代对应SEQID NO：1氨基酸552的位置处的丙氨酸，选自下组的氨基酸取代SEQ ID NO：1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，缬氨酸取代SEQ ID NO:1位置552处的丙氨酸，和选自下组的氨基酸取代SEQ ID NO:1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含：
(i).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺；和/或
(ii).缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸；和/或
(iii).精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含亮氨酸取代对应SEQID NO:1氨基酸522的位置处的谷氨酰胺。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含缬氨酸取代对应SEQID NO:1氨基酸552的位置处的丙氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含精氨酸取代对应SEQID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含：
(i).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，和精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸；或
(ii).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，和缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸；或
(iii).缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸；或
(iv).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(v).缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(vi).精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(vii).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸；或
(viii).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(ix).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(x).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含亮氨酸取代对应SEQID NO:1氨基酸522的位置处的谷氨酰胺，和精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含亮氨酸取代对应SEQID NO:1氨基酸522的位置处的谷氨酰胺，和缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含缬氨酸取代对应SEQID NO:1氨基酸552的位置处的丙氨酸，和精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含亮氨酸取代对应SEQID NO:1氨基酸522的位置处的谷氨酰胺，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含缬氨酸取代对应SEQID NO:1氨基酸552的位置处的丙氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含精氨酸取代对应SEQID NO:1氨基酸572的位置处的甘氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含亮氨酸取代对应SEQID NO:1氨基酸522的位置处的谷氨酰胺，缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含亮氨酸取代对应SEQID NO:1氨基酸522的位置处的谷氨酰胺，缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含亮氨酸取代对应SEQID NO:1氨基酸522的位置处的谷氨酰胺，精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含亮氨酸取代对应SEQID NO:1氨基酸522的位置处的谷氨酰胺，缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
本公开提供了血清白蛋白偶联物，其包含根据本公开的血清白蛋白变体或其功能片段以及化合物。
在一个实例中，本公开的血清白蛋白偶联物相较于包含SEQ ID NO:1中所示血清白蛋白的血清白蛋白偶联具有更长的血清半衰期。本文描述了血清半衰期增加的实例以及用于确定血清半衰期的试验并针对本公开的该实例对其采取必要的调整。
在另一个实例中，本公开的血清白蛋白偶联物相较于包含SEQ ID NO:1中所示血清白蛋白的血清白蛋白偶联物对FcRn的结合亲和力增加。例如，血清白蛋白偶联物对FcRn的结合水平增加至少约2倍或4倍或5倍或10倍。例如，对FcRn的结合水平增加至少约2倍或10倍或40倍或100倍或150倍。本文描述了对FcRn结合亲和力增加的实例以及用于确定相同内容的试验并针对本公开的该实例对其采取必要的调整。
在一个实例中，血清白蛋白变体或其功能片段与另一化合物偶联和/或包封另一化合物。本公开所考虑的化合物可以采取多种形式中的任何一种，包括天然化合物，化学小分子化合物或生物化合物。
在一个实例中，本发明的血清白蛋白变体或其功能片段与化合物偶联，所述化合物直接或间接结合血清白蛋白变体或其功能片段。
示例性的化合物包括蛋白质，含抗体可变区的蛋白质，抗体模拟物，结构域抗体，毒素，放射性同位素，可检测标记物，肽，多肽，胶体，化疗剂，核酸，小分子，反义寡核苷酸，短发夹RNA(shRNA)，siRNA，干扰RNA(RNAi)，核酶，微小RNA，微小RNA适应性shRNA(shRNAmir)，DNA酶及其混合物。在一个实例中，可检测标记物是成像剂。
在一个实例中，化合物是基于蛋白质的化合物，例如，肽，多肽或蛋白质。在一个实例中，蛋白质是治疗性蛋白质。
在另一个实例中，化合物是包含非抗体抗原结合结构域的蛋白质(例如治疗性蛋白质)，如附着连接蛋白(adnectin)，亲和体，阿特里体(atrimer)，EVA蛋白(evasin)，设计的锚蛋白重复蛋白(DARPin)或抗运载蛋白(Anticalin)。
在一个实例中，化合物是包含可变区片段(Fv)的蛋白质(例如，治疗性蛋白质)。例如，蛋白质选自下组：
(i).单链Fv片段(scFv)；
(ii).二聚体scFv(di-scFv)；或
(iii).双抗体；
(iv).三抗体；
(v).四抗体；
(vi).Fab；
(vii).F(ab’)2；
(viii).Fv；或
(ix).与抗体的恒定区、Fc或重链恒定结构域(CH)2和/或CH3相连的(i)-(viii)之一。
在一实例中，蛋白质是抗体或抗原结合片段。
在一个实例中，本发明的抗体或抗原结合片段是重组的，嵌合的，CDR移植的，人源化的，同人源化的(synhumanized)，灵长类化的，去免疫的或人的。
在一个实例中，本公开提供了与血管性血友病因子(von Willebrand factor)或其修饰形式偶联的血清白蛋白变体或其功能片段。例如，该化合物是血管性血友病因子或其修饰形式。在一个实例中，血管性血友病因子包含D′D3结构域。
在一个实例中，本公开提供了与补体抑制剂或其修饰形式偶联的血清白蛋白变体或其功能片段。例如，该化合物是补体抑制剂或其修饰形式。在一个实例中，补体抑制剂选自下组：因子I，(fI)，因子H(fH)，C4b结合蛋白(C4bp)，可溶性CD55(衰变加速因子(DAF))，C1抑制剂(C1-INH或C1酯酶抑制剂)；可溶性CD35(sCR1)；可溶性CD46(膜辅因子蛋白(MCP))，可溶性CD59(保护素)，TT30(CR2-fH)，眼镜蛇毒因子(CVF)及其功能片段或变体。
在一个实例中，补体抑制剂是可溶性补体抑制剂，如sCR1，或其功能片段或变体。在一个实例中，补体抑制剂是变体或修饰型sCR1。
在一个实例中，补体抑制剂是C1抑制剂(即，C1-INH)或其功能片段或变体。在一个实例中，补体抑制剂是修饰型C1-INH的变体。
在一个实例中，本公开提供了与凝血因子偶联的血清白蛋白变体或其功能片段。
在另一个实例中，本公开提供了与结合凝血因子的化合物偶联的血清白蛋白变体或其功能片段。例如，化合物是或结合凝血因子。
在一个实例中，凝血因子选自下组：因子I，因子II(凝血酶原)/凝血酶、因子III、因子V、因子VII、因子VIII、因子IX、因子X、因子XI、因子XII因子XIII和前述任一者的活化形式。例如，凝血因子是因子IX和/或因子IXa。在另一个实例中，凝血因子是因子X和/或因子Xa。在其他实例中，凝血因子是因子IX/IXa和因子X/Xa。在一个实例中，凝血因子是因子VII和/或因子VIIa。在另一个实例中，凝血因子是因子VIII和/或因子VIIIa。
本公开内容还提供了包含本公开的血清白蛋白偶联物和药物运载体和/或赋形剂的组合物。
在一个实例中，相较于包含这样的血清白蛋白偶联物的组合物，该组合物对FcRn的结合亲和力增加，上述血清白蛋白偶联物包含具有SEQ ID NO:1中所示序列的血清白蛋白。
在一个实例中，相较于包含这样的血清白蛋白偶联物的组合物，该组合物的血清半衰期增加，上述血清白蛋白偶联物包含具有SEQ ID NO:1中所示序列的血清白蛋白。
本公开还提供了治疗或预防对象中疾病或病症的方法，所述方法包括给予本公开的血清白蛋白偶联物，或包含血清白蛋白变体或其功能片段的组合物。在一个实例中，该对象有此需要。
在一个实例中，本公开提供了血清白蛋白变体或其功能片段，或血清白蛋白偶联物，或包含该血清白蛋白变体或其功能片段的组合物，用于治疗或预防对象的疾病或病症。
在一个实例中，本公开提供了本公开的血清白蛋白偶联物或包含本公开的血清白蛋白变体或其功能片段的组合物在制备用于治疗或预防对象中疾病或病症的药物中的用途。
在一个实例中，疾病或病症是出血性疾病。
在一个实例中，对象患有出血性疾病。在一个实例中，已经诊断对象患有出血性疾病。在一个实例中，对象正在接受针对出血性疾病的治疗。
在本文所述的任何方法的一个实例中，在发展出出血性疾病之前或之后给予包含本公开的血清白蛋白变体的血清白蛋白偶联物或组合物。在本文所述的任何方法的一个实例中，在发展出出血性疾病之前给予包含本公开的血清白蛋白变体的血清白蛋白偶联物或组合物。在本文所述的任何方法的一个实例中，在发展出出血性疾病之后给予包含本公开的血清白蛋白变体的血清白蛋白偶联物或组合物。
在本文所述的任何方法的一个实例中，在出血事件发生之前或之后给予包含本公开的血清白蛋白变体的血清白蛋白偶联物或组合物。在一个实例中，在出血事件发生之前给予包含本公开的血清白蛋白变体的血清白蛋白偶联物或组合物。在另一个实例中，在出血事件发生之后给予包含本公开的血清白蛋白变体的血清白蛋白偶联物或组合物。
出血事件对于本领域技术人员而言是显而易见的并且包括例如小和/或大出血事件。在一个实例中，出血事件是大出血事件。例如，大出血事件是导致血红蛋白降低≥5g/dL或血细胞比容绝对降低≥15％的任何情况。在一个实例中，出血事件是小出血事件。例如，小出血事件是导致血红蛋白降低≤4g/dL或血细胞比容绝对降低≥10％的任何情况。
在一个实例中，对象具有发展出血性疾病的风险。例如，具有发展出出血性疾病的风险的对象包括但不限于，凝血因子(例如，因子VII和/或因子IX)中具有突变、缺失或重排的那些或患有血小板异常的那些。在一个实例中，对象拥有已经发展出出血性疾病的亲属。例如，出血性疾病是遗传性的。在一个实例中，出血性疾病是获得的。
在一个实例中，在出血性疾病的症状发生之前或之后给予包含血清白蛋白变体的血清白蛋白偶联物或组合物。在一个实例中，在出血性疾病的症状发生之前给予包含血清白蛋白变体的血清白蛋白偶联物或组合物。在一个实例中，在出血性疾病的症状发生之后给予包含血清白蛋白变体的血清白蛋白偶联物或组合物。在一个实例中，包含本公开的血清白蛋白变体的血清白蛋白偶联物或组合物以缓解或减少出血性疾病的一种或多种症状的剂量给予。
出血性疾病的症状对于本领域技术人员而言是显而易见的，包括例如：
·容易瘀伤；
·牙龈出血；
·小切口或牙科治疗引起的大量出血；
·不明原因的流鼻血；
·月经期大量出血；
·关节内出血；和/或
·手术后出血过多。
在一个实施例中，出血性疾病由血液凝固障碍引起。例如，血液凝固障碍是血友病，血管性血友病(von Willebrand disease)，因子I缺乏症，因子II缺乏症，因子V缺乏症，因子V/因子VIII组合型缺乏症，因子VII缺乏症，因子X缺乏症，因子XI缺乏症或因子XIII缺乏症。在一个实例中，血友病是A型血友病或B型血友病。在一个实例中，对象具有需要预防性治疗的病症。
在一个实例中，以降低对象出血严重性的量向对象给予包含本公开的血清白蛋白变体的血清白蛋白偶联物或组合物。
在本文所述的任何方法的一个实例中，对象是哺乳动物，例如灵长类动物，如人。
本文所述的治疗方法可另外包括给予其他化合物以减少、治疗或预防出血性疾病的作用。
本公开还提供了包含结合凝血因子的血清白蛋白变体或其功能片段的组合物，用于治疗或预防出血性疾病。
本公开还提供了包含结合凝血因子的血清白蛋白变体或其功能片段的组合物在制备用于用于治疗或预防出血性疾病的药物中的用途。
本公开还提供了试剂盒，所述试剂盒包括与说明书包装在一起、与凝血因子结合的本公开的至少一种包含血清白蛋白变体或其功能片段的血清白蛋白偶联物或组合物，用于治疗或预防对象中的出血性疾病。任选地，试剂盒还包含治疗活性化合物或药物。
本公开还提供了试剂盒，所述试剂盒包括与说明书包装在一起、与凝血因子结合的包含本公开的血清白蛋白变体或其功能片段的至少一种血清白蛋白偶联物或组合物，以将偶联物或组合物给予患有出血性疾病或处于患出血性疾病风险的对象，任选地，与治疗活性化合物或药物组合。
本文描述了与凝血因子结合的本公开的血清白蛋白偶联物或组合物的示例性作用，并适用于前述五段所述的实例，或需必要的调整。
附图说明
图1是显示注射到表达人FcRn受体的小鼠中的HSA变体的血清HSA浓度的示意图。(μg/mL；平均值±SEM)。
序列表要点
SEQ ID NO:1 人血清白蛋白的氨基酸序列
SEQ ID NO:2 人凝血因子VIII的氨基酸序列
SEQ ID NO:3 人凝血因子IX的氨基酸序列
SEQ ID NO:4 人凝血因子X的氨基酸序列
SEQ ID NO:5 人凝血因子VII的氨基酸序列
SEQ ID NO:6 血管性血友病因子的氨基酸序列
具体实施方式
概述
通篇中，除非另有说明或上下文另有要求，应认为单个步骤、组合物、步骤的组或组合物的组包括一个和多个(即一个或多个)这些步骤、组合物、步骤组或组合物组。
本领域技术人员应理解，本发明易于进行除说明书中所述的那些以外的变化和修改。应理解本发明包含所有这些变化和修改。本发明还包括说明书中单独或共同提到或指出的所有步骤、特征、组合物和化合物，以及所述步骤或特征中任意两种或更多种或任意和全部组合。
本发明的范围不限于本文所述的具体实施例，实施例仅用于示例目的。功能上等同的产品、组合物和方法清楚地包含于本发明的范围内。
本发明的任何实施例都将经必要的修改以适用于本发明的任何其他实施例，除非另有明确说明。换言之，本公开的任何具体实例可以与本公开的其他任何具体实例组合(除非相互排斥)。
将采用公开特定特征或特征组或方法或方法步骤的本公开的任何实例以提供对于免除特定特征或特征组或方法或方法步骤的明确支持。
除非另有明确定义，本文使用的所有技术和科学术语都具有与本领域普通技术人员的常规理解相同的含义(例如在细胞培养、分子遗传学、免疫学、免疫组化、蛋白质化学和生物化学领域)。
除非另有说明，本发明中使用的重组蛋白、细胞培养和免疫技术是标准方法，其是本领域技术人员熟知的。这类技术描述并解释于文献中，例如J.Perbal，《分子克隆实践指南》(A Practical Guide to Molecular Cloning)，约翰韦利森出版社(John Wiley andSons)(1984)，J.Sambrook等，《分子克隆：实验室指南》(Molecular Cloning:A LaboratoryManual)，冷泉港实验室出版社(Cold Spring Harbour Laboratory Press)(1989)，T.A.Brown(编)，《精编分子生物学：实践指南》(Essential Molecular Biology:APractical Approach)，卷1和2，IRL出版社(1991)，D.M.Glover和B.D.Hames(编)，《DNA克隆：实践指南》(DNA Cloning:A Practical Approach)，卷1-4，IRL出版社(1995和1996)，以及F.M.Ausubel等(编)，《新编分子生物学实验指南》(Current Protocols in MolecularBiology)，格林出版联合公司和韦利科学公司(Greene Pub.Associates and Wiley-Interscience)(1988，包括直至今日的所有更新)，Ed Harlow和David Lane(编)，《抗体：实验室手册》(Antibodies:A Laboratory Manual)，冷泉港实验室出版社(1988)，以及J.E.Coligan等(编)，《新编免疫学实验指南》(Current Protocols in Immunology)，约翰韦利森出版社(包括直至今日的所有更新)。
本文中可变区及其部分、免疫球蛋白、抗体及其片段的描述和定义由以下文献中的讨论进一步阐明：Kabat Sequences of Proteins of Immunological Interest(感兴趣的免疫蛋白序列)，马里兰州贝塞斯达，1987和1991，Bork等，J Mol.Biol.242,309-320,1994，Chothia和Lesk J.Mol Biol.196:901-917,1987，Chothia等，Nature 342,877-883,1989和/或Al-Lazikani等，J Mol Biol 273,927-948,1997。
术语“和/或”(例如“X和/或Y”)应理解为表示“X和Y”或“X或Y”且应被认为提供了对这两种含义或各含义的明确支持。
整篇说明书中，词语“包括”或其变化形式，如“包含”或“含有”应理解为意味着包括所指的元素、整数或步骤，或成组的元素、整数或步骤，但不排除任何其它元素、整数或步骤，或成组的元素、整数或步骤。
本文所用术语“来源于”或“源自”表示特定整体可获自特定来源，但并不一定直接来自该来源。
选择的定义
血清白蛋白(或血液白蛋白)是最丰富的血液蛋白并作为血液中类固醇、脂肪酸和甲状腺激素的运载体蛋白质工作，并在稳定胞外流体体积中起主要作用。仅为了命名的目的而非限制，人血清白蛋白的示例性序列示于NCBI GenBank登陆号AEE60908和SEQ ID NO:1中。应当理解的是，述及“血清白蛋白”或“白蛋白”包括前原白蛋白(preproalbumin)，其包含N端肽、原白蛋白(proalbumin)和分泌型白蛋白。氨基酸的位置在本文中通过以由585个氨基酸组成的分泌型白蛋白蛋白质(例如，如SEQ ID NO：1所示)为参照指出。白蛋白包含三个同源结构域，其中各结构域是具有共同结构基序的两个亚结构域的产物。结构域I、II和III可以参照人血清白蛋白(如SEQ ID NO：1所示)定义。例如，结构域I包含SEQ ID NO：1的氨基酸1(±1至15个氨基酸)至194(±1至15个氨基酸)，结构域II包含SEQ ID NO：1的氨基酸192(±1至15个氨基酸)至387(±1至15个氨基酸)，和结构域III包含SEQ ID NO：1的氨基酸残基381(±1至15个氨基酸)至585(±1至15个氨基酸)。短语“±1至15个氨基酸”指氨基酸残基可能与所指氨基酸位置的C末端和/或N末端偏离1或2或3或4或5或6或7或8或9或10或11或12或13或14或15个氨基酸。Dockal等(The Journal of Biological Chemistry,1999,第274(41)卷:29303-29310)和Kjeldsen等(Protein Expression andPurification,1998,第13卷:163-169)描述了示例性结构域I、II和III。
来自其他物种的血清白蛋白(例如，灵长类动物血清白蛋白(如黑猩猩血清白蛋白，大猩猩血清白蛋白)，啮齿动物血清白蛋白(如仓鼠血清白蛋白，豚鼠血清白蛋白，小鼠白蛋白和大鼠血清白蛋白)，牛血清白蛋白，马血清白蛋白，驴血清白蛋白，兔血清白蛋白，山羊血清白蛋白，绵羊血清白蛋白，狗血清白蛋白，鸡血清白蛋白和猪血清白蛋白)的其他序列可以使用本文所提供和/或在公众可及的数据库中的序列确定和/或使用标准技术确定(例如，如Ausubel等,(编辑),《新编分子生物学实验指南》(Current Protocols inMolecular Biology),格林出版联合公司和韦利科学公司(Greene Pub.Associates andWiley-Interscience)(1988，包括直到现在的所有更新)或Sambrook等,《分子克隆：实验室手册》(Molecular Cloning:A Laboratory Manual),冷泉港实验室出版社(Cold SpringHarbor Laboratory Press)(1989)中所述)。
对于SEQ ID NO:1中的氨基酸位置，本文所用短语“对应……”应当理解为指代白蛋白序列内的氨基酸残基或位置，而不一定是包含SEQ ID NO:1的序列。例如，在包含10个氨基酸N-末端截短的白蛋白序列中述及“对应SEQ ID NO:1氨基酸522的位置”将必然指位置512处的氨基酸。在一个实例中，血清白蛋白包含SEQ ID NO:1中所示序列。
述及血清白蛋白的“功能片段”应当理解为指代保留并表现出血清白蛋白功能性(即，结合FcRn的能力)的血清白蛋白片段。片段可以包含白蛋白的一个或更多个结构域，这类结构域的片段或其组合或由上述内容组成。
如本文所用，“氨基酸取代”指用另一种氨基酸替代多肽序列中特定位置处的氨基酸。
如本文所用，术语“FcRn”指新生Fc受体，也称为Brambell受体，并且是β-2-微球蛋白和主要组织相容性复合物I型样Fc受体(FCGRT)截短重链的异二聚体。
如本文所用，术语“变体”或“突变体”或“突变的”指这样的血清白蛋白，所述血清白蛋白经历了使用用于定点诱变的公知技术或任何其他常规方法进行的一个或多个氨基酸取代。
对于血清蛋白质和FcRn的相互作用，本文所用术语“结合”意指该相互作用取决于细胞或蛋白质上存在的特定结构(例如，抗原决定簇或表位)。
如本文所用，述及与血清白蛋白变体和FcRn相互作用有关的“亲和力增加”或“结合增加”或“以更高水平结合”的短语应理解为意指血清白蛋白变体或功能片段以比如SEQID NO：1所示的人血清白蛋白更频繁，更快速，以更长的持续时间和/或更大的亲和力(例如，1.5倍或2倍或5倍或10倍或20倍或40倍或60倍或80倍至100倍或150倍或200倍)与FcRn结合或关联。
出于澄清的目的并且基于本文的示例性主题对于本领域技术人员而言是显而易见的是，在本说明书中述及“亲和力”是指血清白蛋白变体与FcRn的相互作用、结合或关联。
出于澄清的目的并且基于本文的示例性主题对于本领域技术人员而言是显而易见的是，述及“至少大约的亲和力”将理解为意指亲和力等于所述值或更高(即，引用为亲和力的值较低)，即，2nM的亲和力大于3nM的亲和力。换句话说，该术语可以是“X的亲和力或更小”，其中X是本文所引用的值。
如本文所用，在本公开的上下文中，术语“血清半衰期”或“血浆半衰期”指体内血清白蛋白的浓度或量减少50％(即，一半)所需的时间段，例如由于自然机制的降解和/或清除或隔离。本领域技术人员将认识到的是，血清白蛋白的血清半衰期取决于各种生理状况(例如，健康状况，体型/体重)。在健康的人类对象中，血清白蛋白的血清半衰期为19天。用于确定血清白蛋白的血清半衰期的方法是本领域已知的，并且包括例如药代动力学分析。为了本公开的目的，“增加”或“增强的”血清半衰期是指相较于SEQ ID NO：1中所示血清白蛋白，将血清白蛋白变体的血清浓度降低50％所花费的时间的升高或增加。
术语“重组”应理解为指人工遗传重组的产物。因此，对于包含抗体抗原结合结构域的重组蛋白，该术语不包括在对象体内天然产生的抗体，所述抗体为B细胞成熟期间发生的天然重组的产物。然而，如果这类抗体被分离，其应被认为是包含抗体抗原结合结构域的分离的蛋白质。类似地，如果编码该蛋白质的核酸被分离并使用重组方式表达，则所得蛋白质是包含抗体抗原结合结构域的重组蛋白。重组蛋白还包括当其处于细胞、组织或对象(例如蛋白质在其中表达的细胞、组织或对象)内时通过人工重组方式表达的蛋白质。
术语“蛋白质”应理解为包括单条多肽链(即通过肽键连接的一系列相邻氨基酸)或彼此共价或非共价连接的一系列多肽链(即多肽复合物)。例如，可使用合适的化学键或二硫键共价连接该一系列多肽链。非共价键的示例包括氢键、离子键、范德华力和疏水相互作用。
术语“多肽”或“多肽链”应据以上段落理解为表示通过肽键连接的一系列相邻氨基酸。
本文所用术语“抗原结合结构域”应理解为表示能够特异性结合抗原的抗体区域，即，VH或VL或包含VH和VL的Fv。抗原结合结构域不需要在整个抗体的情形下，例如，它可以是分离的(例如，结构域抗体)或另一种形式(例如，如本文所述，如scFv)。
出于本公开的目的，术语“抗体”包括能够通过Fv中包含的抗原结合结构域特异性结合一种或几种密切相关的抗原(例如，凝血因子)的蛋白质。该术语包括四链抗体(例如，两条轻链和两条重链)、重组或修饰的抗体(例如，嵌合抗体、人源化抗体、人抗体、CDR移植抗体、灵长类动物化抗体、去免疫化抗体、同人源化抗体、半抗体、双特异性抗体)。抗体可以是任何类型(如IgG、IgE、IgM、IgD、IgA和IgY)、类(如IgG1、IgG2、IgG3、IgG4、IgA1和IgA2)或亚类。在一个实例中，抗体是鼠(小鼠或大鼠)抗体或灵长类动物(如，人)抗体。在一个实例中，抗体重链缺少C-末端赖氨酸残基。在一个实例中，抗体是人源化的、同人源化的、嵌合的、CFR移植的或去免疫的。
如本文所用，“可变区”指本文所定义抗体的轻链和/或重链的部分，其能够特异性结合抗原并包含互补决定区(CDR)(即CDR1、CDR2和CDR3)和框架区(FR)的氨基酸序列。
本文所用术语“Fv”应理解为指任何如下所述蛋白质，无论其由多个多肽或单个多肽组成：其中轻链的可变区(VL)和重链的可变区(VH)相关联并形成具有抗原结合结构域的复合物(即能够特异性结合抗原)。形成抗原结合结构域的VH和VL可以在单条多肽链中或不同多肽链中。此外，本发明的Fv(以及本发明的任何蛋白质)可具有多个抗原结合结构域，其可结合或不结合相同的抗原。该术语应理解为包括直接来源于抗体的片段以及采用重组方式生产的对应于这类片段的蛋白质。在一些实例中，VH不与重链恒定结构域(CH)1相连和/或VL不与轻链恒定结构域(CL)相连。示例性的含Fv多肽或蛋白质包括Fab片段、Fab’片段、F(ab’)片段、scFv、双抗体、三抗体、四抗体或更高级的复合物，或者与恒定区或其结构域(如CH2或CH3结构域)相连的任意前述物质，如微小抗体。“Fab片段”由免疫球蛋白的单价抗原结合片段组成，且可通过使用木瓜蛋白酶消化全抗体以生成由完整轻链和一部分重链组成的片段来生产或者可使用重组方法来生产。通过使用胃蛋白酶处理全抗体随后还原以生成由完整轻链和一部分重链(包含VH和单个恒定结构域)组成的分子，由此可获得抗体的“Fab'片段”。通过该方式处理，每个抗体可获得两个Fab'片段。还可通过重组方式生产Fab'片段。抗体的“F(ab')2片段”由通过两个二硫键联合在一起的两个Fab'片段的二聚体组成，并可通过使用胃蛋白酶处理全抗体分子而不进行后续还原来获得。“Fab2”片段是包含两个Fab片段的重组片段，这两个Fab片段采用例如亮氨酸拉链或CH3结构域连接。“单链Fv”或“scFV”是含有抗体的可变区片段(Fv)的重组分子，其中轻链的可变区和重链的可变区通过合适的柔性多肽接头共价连接。
抗体的“抗原结合片段”包含完整抗体的一个或多个可变区。抗体片段的示例包括但不限于，Fab、Fab'、F(ab')2和Fv片段；双抗体；线性抗体；单链抗体分子；半抗体和由抗体片段形成的多特异性抗体。
本文所用术语“病症”指对正常功能的破坏或干扰，并不限于任何特定病症，且包括疾病或紊乱。
本文所用术语“出血性病症”或“出血性疾病”指存在血液凝固异常的病症，例如，血液凝固能力降低或不足和/或异常出血(内部和/或外部)，例如，出血过多。
本文所用“凝血因子”指与印迹凝结(blot clot)(即，血液凝固)的形成相关的因子。在一个实例中，凝血因子具有促凝血活性。凝血因子为本领域已知并且包括但不限于，因子I，因子II，因子III，因子V，因子VII，因子VIII，因子IX，因子X，因子XI，因子XII因子XIII和前述中任一者的活化形式。该术语还包括凝血因子的重组形式和/或其修饰形式，例如，如本领域已知的和/或本文所述的。
如本文所用，对象处于发展出疾病或病症或其复发或重新恶化的“风险”可能或可能不具有可检测的疾病或疾病的症状，并且在根据本公开治疗之前可能或可能没有显示出可检测的疾病或疾病的症状。处于“风险”表示对象具有一种或多种风险因素，这些风险因素是与疾病或病症的发展相关的可测参数，如本领域已知和/或本文所述的。
本文所用术语“治疗”或“处理”包括给予本文所述的血清白蛋白变体偶联物从而降低或消除特定疾病或病症的至少一种症状或减缓该疾病或病症的进展。
本文所用术语“预防”、“阻止”或“避免”包括提供关于个体中出血性疾病或出血性疾病的发生或复发的预防。个体可能倾向于或有风险发展出疾病或疾病复发，但尚未被诊断患有该疾病或复发。
“有效量”指按照一定剂量和必要时程至少能够有效实现所需效果的量。例如，所需结果可以是治疗或预防结果。可在一次或多次给药中给予有效量。在本公开的一些实例中，术语“有效量”意指实现对前述疾病或病症治疗所必需的量。在本公开的一些实例中，术语“有效量”意指实现对前述疾病或病症相关的因子变化所必需的量。例如，有效量可能足以影响凝血水平的改变。有效量可以根据待治疗的疾病或病症或待改变的因素以及根据体重、年龄、种族背景、性别，健康和/或身体状况以及与所治疗的哺乳动物相关的其他因素而变化。通常，有效量将落入相对较宽的范围(例如，“剂量”范围)，其可以通过医疗从业者的常规试验和实验确定。因此，该术语不应被解释为将本公开限制于特定量。有效量可以单个剂量或在治疗期间内重复一次或多次的剂量给予。
“治疗有效量”是至少实现特定疾病或病症可测量改善所需的最小浓度。本文所述治疗有效量可以根据诸如患者的疾病状态、年龄、性别和体重等因素以及白蛋白偶联物在个体中引发所需反应的能力而变化。在治疗有效量中，白蛋白偶联物的治疗有益效果胜过任何毒性或有害效果。在一个实例中，治疗有效量应被理解为指足以减少或抑制一种或多种出血性疾病或其并发症的症状的量的白蛋白偶联物。
本文所用术语“预防有效量”应理解为指足以预防或抑制或延迟出血性疾病或其并发症的一种或多种可检测症状发生的量的白蛋白偶联物。
本文所用术语“对象”应理解为指包括人的任何动物，例如哺乳动物。示例性对象包括但不限于人和非人灵长类动物。例如，该对象是人。
血清白蛋白变体
本公开提供了血清白蛋白变体或其功能片段，其相较于SEQ ID NO:1中所示的序列，具有限定的氨基酸取代。在一个实例中，本公开的血清白蛋白变体或其片段包含与本文所公开的序列具有至少约85％或90％或95％或97％或98％或99％相同性的序列，其中所述血清白蛋白变体或其片段结合FcRn，如本文所述，根据任何实例。
本公开提供了血清白蛋白变体或其功能片段，其包含选自下组的一种或多种氨基酸取代：
(i).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，
酪氨酸，缬氨酸和亮氨酸；
(ii).缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸；
(iii).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸；和
(iv).其组合。
在一个实例中，血清白蛋白变体或其功能片段还包含酪氨酸取代对应SEQID NO:1氨基酸573的位置处的赖氨酸。
例如，发明人已经在SEQ ID NO:1中所示的序列中鉴定了数个氨基酸残基，所述氨基酸残基可以被取代，而不丧失功能，或导致功能改善。在一个实例中，血清白蛋白变体或其功能片段相较于SEQ ID NO:1中所示的序列在对应氨基酸522、552和/或572的位置处包含1-3个氨基酸取代。例如，血清白蛋白变体或其功能片段相较于SEQ ID NO:1中所示的序列在对应氨基酸522、552和/或572的位置处包含1或2或3个氨基酸取代。
任选地，血清白蛋白变体或其功能片段相较于SEQ ID NO:1中所示的序列在对应氨基酸573的位置处还包含1个氨基酸取代。在一个实例中，血清白蛋白变体或其功能片段相较于SEQ ID NO:1中所示的序列在对应氨基酸522、552和/或572和任选地573的位置处包含1-4个氨基酸取代。例如，血清白蛋白变体或其功能片段相较于SEQ ID NO:1中所示的序列在对应氨基酸522、552和/或572和任选地573的位置处包含1或2或3或4个氨基酸取代。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的甘氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的异亮氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的甲硫氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的苯丙氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的色氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的酪氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的缬氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的亮氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的丙氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸552的位置处的缬氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸572的位置处的丙氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸572的位置处的谷氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸572的位置处的组氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸572的位置处的丝氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸572的位置处的赖氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸572的位置处的精氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸572的位置处的缬氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的亮氨酸和位于对应SEQ ID NO:1氨基酸572的位置处的精氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的亮氨酸和位于对应SEQ ID NO:1氨基酸552的位置处的缬氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的亮氨酸和位于对应SEQ ID NO:1氨基酸573的位置处的酪氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸552的位置处的缬氨酸和位于对应SEQ ID NO:1氨基酸573的位置处的酪氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸572的位置处的精氨酸和位于对应SEQ ID NO:1氨基酸573的位置处的酪氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的亮氨酸，位于对应SEQ ID NO:1氨基酸552的位置处的缬氨酸，和位于对应SEQ ID NO:1氨基酸572的位置处的精氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的亮氨酸，位于对应SEQ ID NO:1氨基酸552的位置处的缬氨酸，和位于对应SEQ ID NO:1氨基酸573的位置处的酪氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的亮氨酸，位于对应SEQ ID NO:1氨基酸572的位置处的精氨酸，和位于对应SEQ ID NO:1氨基酸573的位置处的酪氨酸。
在一个实例中，本公开的血清白蛋白变体或其功能片段包含SEQ ID NO:1中所示序列的变体，其中所述变体序列至少包含位于对应SEQ ID NO:1氨基酸522的位置处的亮氨酸，位于对应SEQ ID NO:1氨基酸552的位置处的缬氨酸，位于对应SEQ ID NO:1氨基酸572的位置处的精氨酸，和位于对应SEQ ID NO:1氨基酸573的位置处的酪氨酸。
用于产生血清白蛋白的变体形式的示例性方法述于本文或为本领域所知并包括：
·诱变DNA(Thie等,Methods Mol.Biol.525:309-322,2009)或RNA(Kopsidas等,Immunol.Lett.107:163-168,2006；Kopsidas等BMC Biotechnology,7:18,2007；和WO1999/058661)；
·将编码多肽的核酸导入增变细胞(mutator cell)，例如XL-1Red、XL-mutS和XL-mutS-Kanr细菌细胞(司查塔基公司(Stratagene))；
·DNA改组，例如，Stemmer,Nature 370:389-91,1994中所公开；和
·定点诱变，例如，参见Dieffenbach(编)和Dveksler(编)(刊于：《PCR引物：实验室手册》(PCR Primer:A Laboratory Manual)，冷泉港实验室(Cold Spring HarborLaboratories)，纽约，1995)。
用于确定本公开的血清白蛋白变体或其功能片段的生物活性的示例性方法对于本领域技术人员而言将是显而易见的和/或述于本文。例如，本文中描述了用于确定血清白蛋白变体或其功能片段的亲和力(包括亲和力、结合、解离和治疗功效)的方法。
例如，发明人已经在SEQ ID NO:1中所示的序列中鉴定了数个氨基酸残基，所述氨基酸残基可以被取代以增加血清白蛋白的半衰期。例如，血清白蛋白变体或其功能片段包含一个或多个氨基酸取代，所述氨基酸取代增加白蛋白对新生Fc受体(FcRn)的亲和力。在一个实例中，相较于SEQ ID NO:1中所示的血清白蛋白，变体或其功能片段对FcRn的亲和力增加。例如，血清白蛋白变体或其功能片段在较低的pH(例如，约pH 6.0)下对FcRN的亲和力增加，以促进核内体中的白蛋白/FcRn结合。在一个实例中，相较于白蛋白在约pH 7.4下的亲和力，白蛋白在约pH 6.0下对FcRn的亲和力增加，以促进细胞回收后白蛋白再释放到血液中。这些氨基酸取代能够用于延长蛋白质的半衰期，这通过减少从血液的清除。
在一个实例中，示例性的氨基酸取代包括：Q522G、Q522I、Q522K、Q522M、Q522L、Q522F、Q522W、Q522Y、Q522V、A552V、G572A、G572E、G572H、G572S、G572K和G572R。
在另一个实例中，示例性的氨基酸取代包括Q522G、Q522I、Q522K、Q522M、Q522L、Q522F、Q522W、Q522Y、Q522V、Q522A、A552V、G572A、G572E、G572H、G572S、G572K、G572V和G572R。
偶联物
在一个实例中，本公开的血清白蛋白变体或其功能片段与另一化合物偶联和/或包封另一化合物。例如，化合物选自下组：放射性同位素，可检测标记物，治疗性化合物，治疗性蛋白质，显像剂，胶体，毒素，核酸，肽，蛋白质，小分子，反义寡核苷酸，短发夹RNA(shRNA)，siRNA，干扰RNA(RNAi)，核酶，微小RNA，微小RNA适应性shRNA(shRNAmir)，DNA酶及其混合物。
该化合物可以直接或间接地结合血清白蛋白变体或其功能片段(例如，在间接结合的情况下可以包含接头)。化合物的实例包括，放射性同位素(例如，碘131，钇90或铟111)，可检测标记物(例如，荧光团或荧光纳米晶体或量子点)，治疗性化合物或蛋白质(例如，化疗剂或抗炎或凝血因子)，胶体(例如，金)，毒素(例如，蓖麻毒素或破伤风类毒素)，核酸，蛋白质(例如，包含抗体抗原结合结构域的蛋白质)，及其混合物。在一个实例中，血清白蛋白变体或其功能片段与凝血因子偶联。
例如，该化合物是蛋白质并通过胺键与血清白蛋白变体或其功能片段偶联。
在一个实例中，公开内容提供了融合蛋白，其包含血清白蛋白变体或其功能片段和化合物(例如，治疗性蛋白质，诸如凝血因子)。例如，化合物位于血清白蛋白变体或其功能片段的N-末端，血清白蛋白变体或其功能片段的C-末端，插入血清白蛋白变体或其功能片段的环中或其任何组合。
本领域已知并在本文中描述了可以与本公开的血清白蛋白变体偶联的示例性化合物以及用于这类偶联的方法。
放射性同位素
在一个实例中，本公开提供了与放射性同位素偶联的血清白蛋白变体或其功能片段。
适用于本公开的放射性同位素对于本领域技术人员而言是显而易见的并包括，例如，碘123(123I)，碘125(125I)，碘130(130I)，碘133(133I)，碘135(135I)，钪47(47Sc)，砷72(72As)，钪-72(72Sc)，钇90(90Y)，钇88(88Y)，钌97(97Ru)，钯100(100Pd)，铑101m(101mRh)，锑119(119Sb)，钡128(128Ba)，汞197(197Hg)，砹211(211At)，铋212(212Bi)，钐153(153Sm)，铕169(169Eu)，铅212(212Pb)，钯109(109Pd)，铟111(111In)，67Gu，68Gu，铜67(67Cu)，溴75(75Br)，溴76(76Br)，溴77(77Br)，锝99m(99mTc)，碳11(11C)，氮13(13N)，氧15(15O)，碘18(18I)，铼188(188Re)，铅203(203Pb)，铜64(64Cu)，铑105(105Rh)，金198(198Au)，氩199(199Ag)或177(177Lu)。
可检测标记物
在一个实例中，本发明提供了与可检测标记物偶联的血清白蛋白变体或其功能片段。例如，可检测标记物是荧光团，荧光纳米晶体或量子点。
术语“荧光团”是指一种化合物，该化合物吸收特定波长的光并发出较长波长的荧光，或重新发出光。荧光团可以在紫外光谱(10nm至400nm)，可见光谱(400nm至700nm)或近红外区(680nm至100,000nm)中发出荧光。
用于本公开的合适的荧光团对于本领域技术人员而言是显而易见的并且包括例如，吲哚菁绿，IRDye78，IRDye80，IRDye38，IRDye40，IRDye41，IRDye700，IRDye800，IRDye800CW，Cy5，Cy5.5，Cy7，IR-786，DRAQ5NO，Licor NIR，Alexa Fluor488，AlexaFluor680，Alexa Fluor 700，Alexa Fluor750，La Jolla蓝，R-藻红蛋白(PE)，羟基香豆素，甲氧基香豆素，氨基香豆素，荧光素FITC，若丹明Red-X，德克萨斯州红，别藻蓝素(APC)和其类似物。
在一个实例中，可检测标记物是量子点。量子点是一种半导体纳米晶体，具有与尺寸有关的光学和电子特性。适合用作量子点的示例性材料包括，ZnZnS，ZnSe，ZnTe，CdS，CdSe，CdTe，GaΝ，GaP，GaAs，GaSb，InP，InAs，Sb，A1S，A1P，AlAs，AlSb，PbS，PbSe，Ge和Si及其三元和四元混合物。
在一个实例中，可检测标记物是荧光蛋白。用于本公开的合适的荧光蛋白对于本领域技术人员而言是显而易见的并包括，例如，海肾荧光素酶，绿色荧光蛋白(GFP)，青色荧光蛋白(CFP)，红色荧光蛋白(RFP)，蓝色荧光蛋白(BFP)，黄色荧光蛋白(YFB)及其衍生物。
生物实体
凝血因子
本公开提供了与凝血因子偶联的血清白蛋白变体或其功能片段。
血液凝结通过涉及释放多种凝血因子，最终导致形成含有不溶性纤维蛋白的血块阶段的级联进行。示例性的凝血因子包括但不限于，因子I(纤维蛋白原)，因子II(凝血酶原/凝血酶)，因子III(组织因子)，因子V(不稳定因子)，因子VII(前转变素)，因子VIII(抗血友病因子)，因子IX(克雷司马斯因子(Christmas factor))，因子X(斯图亚特因子(Stuart-Prower factor))，因子XI(血浆促凝血酶原酶前体)，因子XII(哈格曼(Hageman)(接触)因子)和因子XIII(纤维蛋白稳定因子/前激肽释放酶(弗莱彻(Fletcher))因子/HMWK(菲茨杰拉德(Fitzgerald))因子)。
例如，该化合物是凝血因子并通过胺键与血清白蛋白变体或其功能片段偶联。
在一个实例中，本公开提供了包含血清白蛋白变体或其功能片段和凝血因子的融合蛋白。例如，凝血因子位于血清白蛋白变体或其功能片段的N-末端，血清白蛋白变体或其功能片段的C-末端，插入血清白蛋白变体或其功能片段的环中或其任何组合。
在一个实例中，凝血因子是因子VIII。出于命名而非限制的目的，人因子VIII的示例性序列示于NCBI参照序列ID NP_000123，蛋白质登录号NM_000132.3中以及SEQ ID NO:2中。
在一个实例中，凝血因子是因子IX。出于命名而非限制的目的，人因子IX的示例性序列示于GenBank ID AAA98726.1中以及SEQ ID NO:3中。
在一个实例中，凝血因子是因子X。出于命名而非限制的目的，人因子X的示例性序列示于Gene ID:2159中以及SEQ ID NO:4中。
在一个实例中，凝血因子是因子VII。出于命名而非限制的目的，人因子VII的示例性序列示于参照序列ID NM_00131中以及SEQ ID NO:5中。
出于命名而非限制的目的，人因子I的示例性序列示于NCBI参照序列ID NM_000508(α链)和NM_005141(β链)，人因子II的示例性序列示于参照序列ID NM_000506，人因子III的示例性序列示于参照序列ID NM_001993，人因子V的示例性序列示于参照序列IDNM_000130，人因子XI的示例性序列示于参照序列ID NM_000128，人因子XII的示例性序列示于参照序列ID NM_000505，人因子XIII的示例性序列示于参照序列ID NM_000129(A链)和NM_001994(B链)。
可以使用本文所提供的序列和/或在公共可及的数据库中确定和/或使用标准技术确定(例如，Ausubel等,(编),《新编分子生物学实验指南》(Current Protocols inMolecular Biology),格林出版联合公司和韦利科学公司(Greene Pub.Associates andWiley-Interscience)(1988，包括直至今日的所有更新)或Sambrook等.,《分子克隆：实验室手册》(Molecular Cloning:A Laboratory Manual)，冷泉港实验室出版社(1989))凝血因子的其他序列。
示例性的凝血因子可以是源自供体的血浆或重组蛋白。例如，凝血因子是源自血浆或重组凝血因子蛋白。例如，治疗性蛋白质选自下组：因子I(纤维蛋白原)，因子II((凝血酶原)/凝血酶)，因子III(组织因子)，因子V(不稳定因子)，因子VII(前转变素)，因子VIIa(例如，
)，因子VIII(抗血友病因子；诸如单链重组因子VIII，例如，如Zollner等,Thromb Res.132:280-287,2013中所述；或血浆来源的因子VIII产品，诸如
或
或重组因子VIII产品，诸如
Fs、
/Refacto
或Hyate:
)，因子IX(克雷司马斯因子，例如，血浆来源的因子IX产品诸如
P、
或
或重组因子IX产品诸如Alphanine
Bebulin
Profilnine
Proplex
或
)，因子X(斯图亚特因子)，因子XI(血浆促凝血酶原酶前体)，因子XII(哈格曼(接触)因子)和因子XIII((纤维蛋白稳定因子/前激肽释放酶(弗莱彻)因子/HMWK(菲茨杰拉德)因子，例如，
P，
或
)。在一个实例中，治疗性蛋白质是血管性血友病因子/FVIII复合物(例如，
或
)。在另一实例中，治疗性蛋白质是凝血酶原(例如，
P/N、
或
)。在另一实例中，治疗性多肽是纤维蛋白原(例如，
P)。
血管性血友病因子
本公开提供了与血管性血友病因子偶联的血清白蛋白变体或其功能片段。
本文所用术语“血管性血友病因子(vWF)”包括天然存在的(天然)VWF，以及其变体，例如，片段，融合蛋白或偶联物，或序列变体，其中已经使一个或多个残基插入、缺失或取代，保留了天然存在的vWF的生物活性。出于命名而非限制的目的，人天然vWF的示例性序列示于NCBI参照序列ID:NP_000543.2和SEQ ID NO:6。本领域技术人员将意识到的是天然vWF包含多个结构域。出于本公开的目的，规定了下述注释：
D1-D2-D'-D3-A1-A2-A3-D4-C1-C2-C3-C4-C5-C6-CK，其中D'结构域由SEQ ID NO:6的氨基酸764-865组成；D3结构域由SEQ ID NO:6的氨基酸866-1242组成；和C1结构域由SEQ ID NO:6的氨基酸2255-2328组成。
在一个实例中，vWF是修饰型或突变型或变体型vWF。例如，用于本公开的修饰型vWF包含D’D3结构域和其修饰形式，如其截短的或突变的形式。例如，修饰型vWF包含SEQ IDNO:6的氨基酸764至1242。
在一个实例中，血管性血友病因子是重组血管性血友病因子。
可溶性补体抑制剂
本公开提供了与可溶性补体抑制剂偶联的血清白蛋白变体或其功能片段。
该补体系统由许多细胞表面和可溶性蛋白质组成，它们在消除外源微生物中起作用，同时还可以保护宿主免受补体相关损伤。补体系统的三个途径包括经典途径(涉及C1q，C1r，C1s，C4，C2和C3组分)，凝集素途径和其他途径。已经描述了四种补体受体，CR1(CD35)、CR2(CD21)、CR3(CD11b/CD18)和CR4(CD11c/CD18)。CR1是血浆蛋白补体系统激活的主要调节剂。
在一个实例中，血清白蛋白变体或其功能片段与可溶性补体抑制剂或其修饰(例如，变体)形式偶联。
用于本公开合适的补体抑制剂对于本领域技术人员而言是显而易见的并包括，例如，因子I，(fI)，因子H(fH)，C4b结合蛋白(C4bp)，可溶性CD55(衰变加速因子(DAF))，C1抑制剂(C1-INH或C1酯酶抑制剂)；可溶性CD35(sCR1)；可溶性CD46(膜辅因子蛋白(MCP))，可溶性CD59(保护素)，TT30(CR2-fH)，眼镜蛇毒因子(CVF)和其功能片段或变体。
在一个实例中，补体抑制剂是可溶性补体受体1(sCR1)，也称为补体受体1型；CD35；C3BR；C3b/C4b受体，和TP10。例如，用于本公开的可溶性补体抑制剂是修饰型或变体型sCR1。sCR1和变体型sCR1分子对于本领域技术人员而言是显而易见的并例如在WO1991016437、WO1994000571和WO1997031944中描述。
在一个实例中，补体抑制剂是C1抑制剂(C1-INH)，也称为C1酯酶抑制剂，丝氨酸蛋白酶抑制剂家族G成员1(SERPING1)，HAE1，HAE2，C1NH和C1IN。例如，用于本公开的补体抑制剂是修饰型或变体型C1-INH。在一个实例中，C1-INH是血浆来源的C1-INH。在一个实例中，C1-INH是重组C1-INH。C1-INH和变体型C1-INH分子对于本领域技术人员而言是显而易见的并包括例如
其他合适的C1-INH和变体型C1-INH分子述于例如WO2016070156中。
毒素
本公开提供了与毒素偶联的血清白蛋白变体或其功能片段。
用于本公开合适的毒素对于本领域技术人员而言是显而易见的并包括，例如，蓖麻毒素，相思豆毒素，白喉毒素，破伤风类毒素，假单胞菌外毒素A(PE)和核糖体失活蛋白，如白树毒素，商陆抗病毒蛋白和皂草素。
化疗化合物
本公开提供了与化疗化合物偶联的血清白蛋白变体或其功能片段。
用于本公开的合适的化疗化合物对于技术人员而言是显而易见的并包括，例如，卡铂，顺铂，环磷酰胺，多西他赛尔(docetaxal)，阿霉素，埃罗替尼(erlotinib)，依托泊苷，氟尿嘧啶，伊立替康，甲氨蝶呤，紫杉醇，托泊替康，长春新碱，长春碱，甲氨蝶呤，l-天冬酰胺酶，长春新碱，阿霉素，道诺霉素(doxorubicin)，阿糖胞苷，伊达比星，米托蒽醌，环磷酰胺，氟达拉滨，苯丁酸氮芥及其衍生物。
抗体或抗原结合片段
在一个实例中，本公开提供了与抗体或其抗原结合片段偶联的血清白蛋白变体或其功能片段。
用于本公开的示例性抗体或其抗原结合片段在本文中描述或为本领域所知，并包括：
·人源化抗体或其片段，例如，包含人样可变区的蛋白质，其包括来自移植或插入来自人抗体的FR的非人类物种(例如，小鼠或大鼠或非人类灵长类动物)的抗体的CDR(例如，通过US5225539、US6054297、US7566771或US5585089中所述方法产生)。
·人抗体或其片段，例如，具有存在于人(例如，人种系或体细胞)或来自使用这类区域产生的文库的可变和(任选地)恒定抗体区域的抗体。“人”抗体可以包括未由人序列编码的氨基酸残基，例如，通过体外随机或定点突变引入的突变(例如，通过US5565332中所述方法产生的)和这类抗体的亲和力成熟形式。
·同人源化蛋白或其片段，例如，包含来自新世界(New World)灵长类动物抗体可变区的FR和来自非新世界灵长类动物抗体可变区的CDR(例如，通过WO2007019620中所述的方法产生)。
·灵长类化抗体或其片段，例如，包含来自非人灵长类动物(例如，猕猴(cynomolgus macaque))免疫后产生的抗体的可变区的抗体(例如，通过US6113898中所述的方法产生)。
·嵌合抗体或嵌合抗原结合片段，例如，这样的抗体或片段，其中一个或多个可变结构域来自特定物种(例如，鼠类，诸如小鼠或大鼠)或属于特定抗体类型或亚类，而抗体或片段的其余部分来自另一个物种(例如，人或非人灵长类动物)或属于另一个抗体类型或亚类(例如，通过US6331415、US5807715、US4816567和US4816397中所述的方法产生)。
·去免疫抗体或其抗原结合片段，例如，这样的抗体和片段，其具有一个或多个表位，例如，B细胞表位或T细胞表位被去除(即，经突变)，从而降低对象针对抗体或蛋白质产生免疫应答的可能性(例如，如WO2000034317和WO2004108158中所述)。
·双特异性抗体或其片段，例如，包含对不同抗原或表位具有特异性的两种类型的抗体或抗体片段(例如，两个半抗体)的抗体(例如，如US5731168中所述)。
用于本公开的其他示例性抗体片段在本文中描述或为本领域所已知，并包括：
·单结构域抗体(结构域抗体或dAb)，例如，包含全部或部分抗体重链可变域的单个多肽链。
·双抗体、三抗体、四抗体或更高阶的蛋白质复合物(例如，如WO98/044001和/或WO94/007921中所述)。
·单链Fv(scFv)片段，例如，这样的片段，其在单个多肽链中包含VH和VL区域以及VH和VL之间的多肽接头，这使得scFv能够形成抗原结合所需的结构(即，用于使单个多肽链的VH和VL彼此结合形成Fv)。
·半抗体或半分子，例如，包含单个重链和单个轻链的蛋白质。
本发明还涉及其他抗体和抗体片段，诸如：
(i).微抗体(minibody)，例如，US5837821中所述；
(ii).异源偶联蛋白，例如，US4676980中所述；
(iii).使用化学交联剂产生的异源偶联蛋白，例如，US4676980中所述；和
(iv).Fab3(例如，如EP19930302894中所述)。
蛋白质支架
在一个实例中，本公开提供了与蛋白质支架偶联的血清白蛋白变体或其功能片段。在一实例中，蛋白质支架是免疫球蛋白或免疫球蛋白片段。
用于本公开合适的蛋白质支架在本文中描述或对于本领域技术人员而言是显而易见的，并包括：
·重链免疫球蛋白，例如，不包含轻链的免疫球蛋白(例如，抗体)(例如，如WO9404678、WO9749805和WO 9749805中所述)。
·V样蛋白，例如，包含两个V结构域的T细胞受体，所述V结构域结合成类似于抗体Fv模块的结构(例如，Novotny等,Proc Natl Acad Sci USA 88:8646-8650,1991、WO1999045110或WO2011107595中所述)。
·附着连接蛋白(adnectin)，例如，对基于人纤连蛋白第十纤连蛋白III型(10Fn3)结构域的免疫球蛋白进行改变以赋予抗原结合(例如，如在US20080139791或WO2005056764中所述)。
·抗运载蛋白(Anticalin)，例如，源自脂质运载蛋白的免疫球蛋白，所述脂质运载蛋白具有刚性β-折叠二级结构，并在锥形结构的开口端具有多个环，其可被工程化改造以结合抗原(例如，US7250297或US20070224633中所述)。
·亲和体，例如，源自金黄色葡萄球菌(Staphylococcus aureus)蛋白A的Z结构域(抗原结合结构域)的支架，可以对其进行工程改造以结合抗原(例如，如EP1641818中所述)。
·高亲合性多聚体(avimer)，例如，源自A结构域支架家族的多结构域蛋白(例如，如在WO2002088171中所述)。
·设计的锚蛋白重复蛋白(DARPin)，例如，源自这样蛋白质的锚蛋白家族，所述蛋白质介导膜内在蛋白与细胞骨架的连接，其可以经工程改造以结合不同的靶抗原(例如，如US20040132028中所述)
小分子
在一个实例中，本公开提供了与小分子偶联的血清白蛋白变体或其功能片段。可以从文库中分离这样的小分子。化学小分子文库是可商购的，或者可以使用本领域已知的方法来生成，例如，US5463564中所述的那些。
用于合成小的有机化合物的技术将根据化合物的不同而变化，但是，这类方法对于本领域技术人员而言是已知的。
在一个实例中，使用信息学由已知化合物中选择合适的化学结构单元，以产生组合文库。例如，QSAR(定量结构活性关系)建模方法使用化合物的回归树或线性回归以确定适用性。化学计算集团(Chemical Computing Group,Inc.)(加拿大蒙特利尔)的软件使用关于活性和非活性化合物的高通量筛选实验数据，以创建概率QSAR模型，随后将其用于选择先导化合物。二进制QSAR方法基于形成特定化合物是否将进行所需功能可能性的“描述符”的化合物的三个特征：部分电荷，摩尔折射率(结合相互作用)和logP(分子的亲脂性)。各原子在分子中有一个表面积，并具有与之关联的这三个特性。确定在某些范围内具有部分电荷的化合物的所有原子，并将表面积(范德壁表面积(Van der Walls Surface Area)描述符)相加。然后，将二进制QSAR模型用于生成活动模型或ADMET模型，将其用于构建组合文库。因此，在初始筛选中鉴定出的先导化合物可以用于扩展进行筛选的化合物的列表，从而鉴定具有高活性的化合物。
基于核酸的试剂
在一个实例中，本公开提供了与基于核酸的试剂偶联的血清白蛋白变体或其功能片段。合适的试剂对于本领域技术人员而言是显而易见的并包括，例如，反义寡核苷酸，短发夹RNA(shRNA)，siRNA，干扰RNA(RNAi)，核酶，微小RNA和DNA酶。
反义寡核苷酸
在一个实例中，基于核酸的试剂是反义寡核苷酸或反义核酸。
术语“反义寡核苷酸”或“反义核酸”应被理解为意指与编码如本公开的任何示例中所述的多肽的特定mRNA分子的至少一部分互补并且能够干扰转录后事件如mRNA翻译的DNA或RNA或其衍生物(例如，LNA或PNA)或其组合。反义方法的使用在本领域中是已知的(参见例如，Hartmann和Endres(编辑)，《反义方法手册》(Manual of AntisenseMethodology)，Kluwer出版社(1999))。
本公开中的反义核酸在生理条件下与靶核酸杂交。反义核酸包括对应于结构基因或编码区的序列或对应于影响对基因表达或剪接的控制的序列。例如，反义核酸可以对应于核酸的靶向编码区或5'非翻译区(UTR)或3'-UTR或它们的组合。其可能与在转录过程之中或之后被剪接掉的内含子序列部分互补，例如仅与靶基因的外显子序列互补。反义序列的长度应为至少19个连续核苷酸，例如，核酸的至少50个核苷酸，如至少100、200、500或1000个核苷酸。可以使用与整个基因转录本互补的全长序列。长度可以是100-2000个核苷酸。反义序列与靶转录本的相同性程度应至少为90％，例如95-100％。
催化性核酸
在一个实例中，基于核酸的试剂是催化性核酸。
术语“催化性核酸”是指特异性识别不同的底物并催化该底物的化学修饰的DNA分子或含DNA分子(在本领域中也称为“脱氧核酶”或“DNA酶”)或RNA或含RNA分子(也称为“核酶”或“RNA酶”)。催化性核酸中的核酸碱基可以是碱基A、C、G、T(以及用于RNA的U)。
通常，催化性核酸含有用于特异性识别靶核酸的反义序列和切割酶活性的核酸(本文中也称为“催化结构域”)。在本公开中有用的核酶类型是锤头核酶和发夹核酶。
RNA干扰
在一个实例中，基于核酸的试剂是小干扰RNA(“siRNA”)分子。
RNA干扰(RNAi)能够用于特异性抑制特定蛋白质的产生。不受限于理论，该技术依赖于dsRNA分子的存在，所述dsRNA分子包含与目的基因或其部分的mRNA基本相同的序列。方便地，dsRNA可以在重组载体宿主细胞中由单个启动子产生，其中正义和反义序列侧接无关序列，从而使正义和反义序列能够杂交以形成dsRNA分子，其具有形成环状结构的无关序列。对于本公开合适的dsRNA分子的设计和生产完全在本领域技术人员的能力范围内。
杂交的正义和反义序列的长度应分别为至少19个连续核苷酸，例如至少30或50个核苷酸，例如至少100、200、500或1000个核苷酸。可以使用与整个基因转录产物相对应的全长序列。长度可以是100-2000个核苷酸。正义和反义序列与靶转录产物的相同性程度应为至少85％，例如，至少90％，如95-100％。
示例性的小干扰RNA(“siRNA”)分子包含与靶mRNA约19-21个连续核苷酸相同的核苷酸序列。例如，siRNA序列以二核苷酸AA开头，包含约30-70％的GC含量(例如，30-60％，如40-60％，例如约45％-55％)，并且与任何核苷酸序列都不具有高百分比相同性，除了其将被引入的对象基因组中的靶标之外，例如通过标准BLAST检索确定。
测定血清白蛋白变体的活性
例如，如下文所述，容易筛选本公开的血清白蛋白变体的生物学活性。
确定亲和力
任选地，确定血清白蛋白变体或其功能片段的解离常数(Kd)或结合常数(Ka)或亲和力常数(KD)。
亲和力测量可以通过标准方法来确定，例如，免疫测定，表面等离子共振(SPR；例如，使用BIAcore表面等离子体共振(BIAcore有限公司(BIAcore,Inc.)，新泽西州皮斯卡特维)(Rich和Myszka Curr.Opin.Biotechnol 11:54,2000；Englebienne Analyst.123:1599,1998)，等温滴定量热法(ITC)或本领域已知的其他动力学相互作用试验。
在一些实例中，相较于，血清白蛋白变体或其功能片段具有与SEQ ID NO:1中所示的血清白蛋白相似的KD或与之相比改善的KD(即，KD值比其低)。
对FcRn的结合亲和力还可以使用流式细胞术非定量地确定。例如，稳定表达血清白蛋白变体或其功能片段的CHO细胞在酸性(pH 5.5)和中性(pH 7.4)pH下用alexa-488标记的FcRn/β2m(检测靶标结合)和抗myc-alexa 647(检测表达)染色，并通过流式细胞术进行分析。例如，通过计算相对于未修饰的血清白蛋白(例如，如SEQ ID NO:1所示)的平均荧光强度来确定对FcRn/β2m的相对结合。
确定半衰期
相较于SEQ ID NO：1中所示的血清白蛋白(即，未修饰的血清白蛋白)，本公开所涵盖的血清白蛋白变体或其功能片段具有改善的半衰期，例如，经修饰以延长其半衰期。用于确定半衰期延长的血清白蛋白变体或其功能片段的方法对于本领域技术人员而言是显而易见的。例如，评估了血清白蛋白变体或其功能片段结合新生Fc受体(FcRn)的能力。在这方面，对FcRn增加的结合亲和力增加了血清白蛋白变体或其功能片段的血清半衰期(参见例如，Kim等,Eur J Immunol.,24:2429,1994)。
本公开的血清白蛋白变体或其功能片段的半衰期也可以通过药代动力学研究来测量，例如，根据Kim等,Eur J of Immunol 24:542,1994所述的方法。根据该方法，将蛋白质静脉内注射到小鼠中，并随时间定期测定其血浆浓度，例如，在注射后3分钟至72小时。如此获得的清除曲线应该是双相的，即有α相和β相。为了确定蛋白质的体内半衰期，计算β相中清除率，并将其与野生型或未修饰的蛋白质(即，如SEQ ID NO：1中所示)的清除率进行比较。
体外细胞试验
多种体外试验能够用于评估血清白蛋白变体或其功能片段治疗本文所述疾病或病症的能力。
在一个实例中，在体外细胞试验中测试血清白蛋白变体或其功能片段的摄取和回收。
评估细胞摄取和回收的方法为本领域所知和/或在本文中举例说明。例如，将荧光标记的血清白蛋白变体与在细胞表面表达人FcRn受体的细胞一起孵育。添加标记的血清白蛋白变体后，可以追踪蛋白质回收的进程并通过包括流式细胞术和荧光显微镜(例如，共聚焦荧光显微镜)在内的方法将其与未修饰的血清白蛋白进行比较。可以鉴定并表征特定血清白蛋白变体正常回收途径的变化。
将发现有效回收的血清白蛋白变体或其功能片段鉴定为本公开的变体。
药代动力学分析
在一个实例中，将评估血清白蛋白变体或其功能片段的药代动力学(PK)性质。
评估PK特性的方法为本领域所知和/或在本文中举例说明。例如，将血清白蛋白变体注射到表达人FcRn受体的转基因小鼠或其他合适的哺乳动物宿主(例如，大鼠，食蟹猴)。在一个实例中，表达人FcRn受体的转基因小鼠是“hFcRn Tg32”纯合小鼠(即，B6.Cg-Fcgrttm1Dcr Tg(FCGRT)32Dcr/DcrJ；杰克逊实验室库存号014565；或如Roopenian等,J.Immunol 2003；170:3528-3533中所述)。血清白蛋白的血浆水平将使用可商购的方法使用ELISA评估。
药物组合物
合适地，在用于向对象给予本公开的血清白蛋白变体或其功能片段的方法或组合物中，本公开的血清白蛋白偶联物(即，与化合物偶联的血清白蛋白变体或其功能片段)与药学上可接受的运载体组合，如本领域中所理解的。因此，本公开的一个实例提供了这样的组合物(例如，药物组合物)，其包含与药学上可接受的运载体组合的本公开的血清白蛋白偶联物。
概括地，述及“运载体”意指可以安全地给予任何对象(例如，人)的固体或液体填充剂，粘合剂，稀释剂，包封物质，乳化剂，润湿剂，溶剂，悬浮剂，包衣或润滑剂。取决于给药的具体途径，可以使用本领域已知的各种可接受的运载体，例如，《雷明顿药物科学》(Remington's Pharmaceutical Sciences)(马克出版公司(Mack Publishing Co.)美国新泽西州,1991)中所述的。
本公开的血清白蛋白偶联物能够用于肠胃外，局部，口服或局部给药，气雾剂给药或经皮给药，用于预防或治疗处理。在一个实例中，肠胃外，如皮下或静脉内给予血清白蛋白偶联物。例如，静脉内给予血清白蛋白偶联物。
待给予的血清白蛋白偶联物的制剂将根据所选择的给药途径和制剂(例如，溶液、乳剂、胶囊)而变化。可以在生理上可接受的运载体中制备包含待给予的血清白蛋白偶联物的合适药物组合物。对于溶液或乳剂，合适的运载体包括，例如，水溶液或醇/水溶液、乳液或悬浮液，包括盐水和含缓冲的介质。胃肠道外载剂可以包括氯化钠溶液、林格右旋糖、右旋糖和氯化钠、乳酸林格溶液或非挥发性油。各种合适的水性运载体是本领域技术人员已知的，包括水、含缓冲的水、含缓冲的盐水、多元醇(例如甘油、丙二醇、液体聚乙二醇)、右旋糖溶液和甘氨酸。静脉内载剂可以包括各种添加剂，防腐剂或流体，营养物质或电解质补充剂(通常参见，《雷明顿药物科学》(Remington's Pharmaceutical Science),第16版，Mack编，1980)。组合物可以如所需任选地包含药学上可接受的辅助物质以接近生理条件，如pH调节和缓冲剂和毒性调节剂，例如，乙酸钠、氯化钠、氯化钾、氯化钙和乳酸钠。根据本领域已知的冻干和重建技术，血清白蛋白偶联物可以在使用前冻干储存并在合适的运载体中重建。
待治疗的病症
如本文所讨论，本公开提供了治疗或预防对象中疾病或病症的方法，所述方法包括向有此需要的对象给予本公开的血清白蛋白偶联物或本公开的组合物。在一个实例中，本公开提供了在有此需要的对象中治疗疾病或病症的方法。
本公开还提供了本公开的血清白蛋白偶联物用于治疗或预防对象中疾病或病症的用途，包括向有此需要的对象给予本公开的血清白蛋白偶联物或本公开的组合物。在一个实例中，本公开提供了本公开的血清白蛋白偶联体用于治疗有此需要的对象中疾病或病症的用途。
在一个实例中，疾病或病症是出血性疾病。
在一个实例中，对象患有出血性疾病。出血性疾病可以遗传的或获得的。例如，患有出血性疾病的对象经受出血性疾病的症状，如：
·容易瘀伤；
·牙龈出血；
·小切口或牙科治疗引起的大量出血；
·不明原因的流鼻血；
·月经期大量出血；
·关节内出血；和/或
·手术后出血过多。
在一个实例中，对象具有发展出血性疾病的风险。如果患者发生出血性的风险高于对照群体，则对象处于危险之中。对照群体可以包括从一般人群中随机选择的一个或多个对象(例如，年龄、性别、种族和/或种族匹配)，其未具有或患有心绞痛、中风和/或心脏病发作的家族史。如果发现与出血性疾病相关的“危险因素”与该对象关联，那么可以认为该对象处于出血性疾病的风险。危险因素可以包括与给定疾病相关联的任何活动，性状，事件或特性，例如，通过对对象群体进行统计或流行病学研究。因此，即使鉴定潜在危险因素的研究并未明确包括该对象，也可以将该对象归类为处于出血性疾病的风险。例如，出血过多的对象处于发展出出血性疾病的风险，因为相较于没有出血过多的对象，出血过多的对象群体中出血性疾病的频率增加。
在一个实例中，对象处于发展出出血性疾病的风险，并在出血性疾病的症状发生之前或之后给予血清白蛋白偶联物。在一个实例中，在出血性疾病的症状发生之前给予血清白蛋白偶联物。在一个实例中，在出血性疾病的症状发生之后给予血清白蛋白偶联物。在一个实例中，以减缓或降低处于风险的对象的出血性疾病的一个或多个症状的剂量给予本公开的血清白蛋白偶联物。
本公开的方法可以容易地应用于对象中任何形式的出血性疾病。
本公开的方法还可包括共同给予根据本公开的血清白蛋白偶联物与给予另一治疗有效的试剂以预防或治疗出血性疾病。
在一个实例中，本公开的血清白蛋白偶联物与当前正在使用或研究用于预防或治疗出血性疾病的至少一种其他已知化合物或治疗性蛋白质联用。用于治疗出血性疾病的化合物是本领域已知的。示例性的治疗性蛋白质可以是源自供体的血浆或重组蛋白。例如，治疗性蛋白质是源自血浆或重组凝血因子蛋白。例如，治疗性蛋白质选自下组：因子I，因子II((凝血酶原)/凝血酶)，因子III，因子V，因子VII，因子VIIa(例如，
)，因子VIII(如单链重组因子VIII，例如，如Zollner等,Thromb Res.132:280-287,2013中所述，或血浆来源的因子VIII产品，如
或
或重组因子VIII产品，如
Fs，
/Refacto
或Hyate:
)，因子IX(例如，源自血浆的因子IX产品，如
P，
或
或重组因子IX产品，如Alphanine
Bebulin
Profilnine
Proplex
或
)，因子X，因子XI，因子XII和因子XIII(例如，
P，
或
)。在一个实例中，治疗性蛋白质是血管性血友病因子/FVIII复合物(例如，
或
)。在另一实例中，治疗性蛋白质是凝血酶原(例如，
P/N、
或
)。在另一实例中，治疗性多肽是纤维蛋白原(例如，
P)。在一个实例中，治疗性蛋白质是凝血因子的修饰形式，例如，如本文所述的。
从上文将显而易见，本公开提供了伴随(concomitant)治疗处理对象的方法，其包括向有此需要的对象给予有效量的第一物质和第二物质，其中所述第一物质是本公开的血清白蛋白偶联物，第二物质还用于预防或治疗出血性疾病。
如本文所用，短语“伴随治疗处理”中的术语“伴随”包括在第二药剂存在下给予第一药剂。伴随治疗处理方法包括其中共同给予第一、第二、第三或其他试剂的方法。伴随治疗处理还包括这样的方法，所述方法在第二或其他物质存在的情况下给予第一或其它物质，其中所述第二或其它物质可以，例如，先前已经给予过。伴随治疗处理可以由不同的参与者逐步执行。例如，一个参与者可以给予对象第一试剂，而第二参与者可以给予对象第二试剂，并且给药步骤可以同时或几乎同时或在远隔的时间执行，只要第一试剂(和/或其他试剂)是在第二试剂(和/或其他试剂)存在下的情况下之后给予。参与者和对象可以是同一实体(例如，人)。
可以根据本领域技术人员已知的方法凭经验确定所选介质中活性成分的最佳浓度，并且这将取决于所需的最终药物制剂。
本公开的血清白蛋白偶联物的给药剂量范围是大到足以产生所需效果的剂量范围。例如，组合物包含有效量的血清白蛋白偶联物。在一个实例中，组合物包含治疗有效量的血清白蛋白偶联物。在另一个实例中，组合物包含预防有效量的血清白蛋白偶联物。
剂量不应太大而引起不良副作用，如反常性出血和抑制剂的发展。通常，剂量将随年龄，状况，性别和患者中的疾病的程度变化，并且可以由本领域技术人员确定。在任何并发症发生的情况下，剂量可以由个别医师调整。
剂量可以变化，从约0.1mg/kg至约300mg/kg，例如，从约0.2mg/kg至约200mg/kg，如从约0.5mg/kg至约20mg/kg，每天一次或多次给药，持续一天或数天。
在一些实例中，以高于后续(维持剂量)的初始(或加载)剂量给予血清白蛋白偶联物。例如，以约10mg/kg至约30mg/kg的初始剂量给予v。然后，以约0.0001mg/kg至约10mg/kg的维持剂量给予结合蛋白。维持剂量可以每7-35天给予，如每7或14或28天给予。
在一些实例中，使用剂量递增方案，其中初始以比后续剂量中使用的剂量更低的剂量来给予血清白蛋白偶联物。该剂量方案能够用于对象最初遭受不良事件的情况下。
在对象未对治疗产生适当应答的情况下，可在一周内给予多重剂量。或者，可以给予增加的剂量。
通过给予多于一次暴露或一组剂量，如至少约两次暴露于结合蛋白，例如，约2-60次暴露，更具体为约2-40次暴露，最具体为约2-20次暴露，可以用血清白蛋白偶联物再次治疗对象。
在一个实例中，当疾病的迹象或症状复发时，例如出血发作，可以给予任何再治疗。
在另一实例中，可以限定的间隔给予任何再治疗。例如，后续暴露可以各种间隔给予，例如，约24-28周或48-56周或更长时间。例如，以约24-26周或约38-42周或约50-54周的间隔给予这种暴露。
在对象未对治疗产生适当应答的情况下，可在一周内给予多重剂量。或者，可以给予增加的剂量。
在另一个实施例中，对于经历不良反应的对象，可将初始(或加载)剂量分割为一周内的数天或连续数天。
根据本公开的方法给予血清白蛋白偶联物可以是连续的或间断的，例如，这取决于受体的生理状况，给药的目的是治疗性或预防性的，以及熟练的从业人员已知的其它因素。给药可以在预选的一段时间内基本连续，或者可以是一系列间隔的剂量，例如，在病症发展期间或之后。
试剂盒和其他物质组成
本公开的另一个实例提供了含有本公开血清白蛋白偶联物的试剂盒，其能够用于治疗或预防如上所述的出血性疾病。
在一个实例中，试剂盒包含(a)容器，该容器包含血清白蛋白偶联物，其任选地在药学上可接受的运载体或稀释剂中；和(b)带有治疗或预防对象中出血性疾病的说明书的包装。
在一个实例中，试剂盒包含(a)至少一种血清白蛋白偶联物；(b)将试剂盒用于治疗或预防对象中出血性疾病的说明书；和(c)任选地，至少一种其他治疗活性化合物或药物。
根据本公开的该实例，包装插页在容器上或与容器相关联。合适的容器包括例如瓶，小瓶，注射器等。该容器可以由多种材料形成，例如，玻璃或塑料。容器装载或包含有效治疗或预防出血性疾病的组合物，并且可具有无菌进入端口(例如，所述容器可以是具有皮下注射针可刺穿塞子的静脉输液袋或小瓶)。组合物中至少一种活性剂是血清白蛋白偶联物。标签或包装插页指示该组合物是用于治疗符合治疗条件的对象，例如，患有或倾向于患出血性疾病的对象，并提供关于血清白蛋白偶联物和任何其他药物的给药量和间隔的具体指导。试剂盒还包含其他容器，其包含药学上可接受的稀释缓冲剂，如抑菌注射用水(BWFI)，磷酸盐缓冲盐水、林格溶液和/或右旋糖溶液。试剂盒还可以包括就商业和用户角度而言所需的其它材料，包括其他缓冲液，稀释剂，过滤器，针头和注射器。
任选地，试剂盒还包含含有第二药物的容器，其中所述血清白蛋白偶联物是第一药物，并且该制品还包括用于以有效量使用第二药物治疗对象在包装插页上的说明书。该第二药物可以是前述的治疗性蛋白质。
本公开包括以下非限制性实施例。
实施例
实施例1：人血清白蛋白变体的生成
使用人血清白蛋白的标准易错PCR生成人血清白蛋白(HSA)随机突变的变体的文库。如Gerth等(Protein Eng Des Sel 2004 17(7):595-602)中之前所述，使用基于内含肽的开放阅读框(ORF)选择去除截短和移码变体。
然后将HSA变体克隆亚克隆并转染至Flp-InTM CHO细胞(英杰公司(Invitrogen))以生成转染的稳定细胞系的文库，其各自包含突变白蛋白融合蛋白的单一拷贝。简言之，获得了包含整合的Flp重组靶(FRT)位点的Flp-InTM CHO宿主细胞系。在人CMV启动子的控制下，将HSA变体文库克隆到与血小板衍生生长因子受体(PDGFR)跨膜结构域和Myc标签同框的pcDNA5/FRT表达质粒中。将含有HSA文库和pOG44质粒的pcDNA5/FRT载体共转染到Flp-InTM宿主细胞系中，所述pOG44质粒在人CMV启动子控制下组成性表达Flp重组酶，这导致所有转染的细胞成功进行了Flp催化的重组，并携带一个拷贝的突变白蛋白融合蛋白。HSA变体作为具有PDGFR跨膜区的融合蛋白表达，可在哺乳动物细胞表面上胞外展示膜栓系的变体。稳定转染的细胞在选择培养基中生长约14天以去除未转染的细胞。
实施例2：鉴定与对FcRn/β2m的亲和力增加相关的残基
为了确定HSA变体对新生Fc受体(FcRn/β2m)的结合亲和力，将使用alexa-488标记的FcRn/β2m(在pH5.4下为10μg/ml且在pH7.3下为100μg/ml；以检测靶结合)和抗-myc-alexa 647(以检测构建体的表达)在pH5.4和pH7.3下对稳定表达HSA变体的CHO细胞的各个集合染色，并通过流式细胞仪分析。将与表达各种HSA变体的细胞结合的标记的FcRn的数量定量为染色的细胞的几何平均荧光强度(geoMFI)数据，减去由于标记的FcRn对细胞的非特异性结合所引起的背景荧光，并相较于野生型HSA和HSA变体K573Y确定对FcRn/β2m的相对结合(述于Anderson等.(2014)J Biol Chem,289:13492中)。
根据亲和力选择两个克隆(克隆3.9和克隆5.6)进行进一步分析，并检查各克隆内的单个突变以确定各突变对亲本克隆总体亲和力的贡献。
通过流式细胞术在两个独立的实验中测量对于各HSA变体的FcRn结合。将与表达HSA变体的细胞结合的标记的FcRn的数量定量为染色的细胞的几何平均荧光强度(geoMFI)。从获得的值中减去由于标记的FcRn与细胞的非特异性结合所引起的背景荧光。对于阳性对照HSA变体K573Y以及具有单取代Q522L、G572R和A552V的HSA变体，在pH5.4下观测到相比野生型对FcRn/β2m改善的结合。如表1所示，许多克隆并未显示出相比野生型的结合改善，包括T133I、K162N、K317E、F377I、I388T、F157L、P282S和Y452S。在pH 7.3下，没有一个克隆显示出对FcRn/β2m明显的结合。
实施例3：具有单氨基酸取代的HSA变体的生成
选择氨基酸残基Q522、G572和A552作为感兴趣的残基。生成这样的一组HSA变体，其在残基Q522或G572上具有对每个氨基酸(半胱氨酸除外)的单取代，并在CHO细胞中稳定表达。如上所述，在四个独立的实验中通过流式细胞术确定了HSA变体与FcRn/β2m的结合。将与表达各HSA变体的细胞结合的标记的FcRn的数量定量为染色的细胞的几何平均荧光强度(geoMFI)数据。减去由于标记的FcRn与细胞的非特异性结合所引起的背景荧光，并计算针对各实验确定的均值的置信区间上限和下限(95％CI)。
将pH 5.5和pH 7.4下所有HSA变体的FcRn结合强度(geoMFI)分别标准化以调整实验之间测量的强度的系统差异。对于两种pH条件，将给定HSA变体结合的重复测量值调整为重复之间的平均值(类似于如Dudoit等2002Statistica Sinica 12,111-139中所述的微阵列数据的强度标准化)。为了在pH 5.5下测量FcRn结合，在对于所有测试的变体的geoMFI值范围内，重复均具有明显的非线性差异。通过对各重复的结合强度相对均值(对于4个重复)的结合强度进行稳健回归，将二次函数拟合，并且所有geoMFI值处于log2量级。通过调整，将各预测的实验特异性结合强度替换为跨实验均值结合强度，而各变体的残基保持不变。为了测量在pH 7.4下的FcRn结合，将线性函数拟合(即，调节步骤等同于减去实验特异性(小的)截距常数再除以实验特异性比例常数)。
九个Q522变体在酸性pH 5.5下显示出相对于野生型HSA统计学上显著增加的FcRn/β2m结合：Q522G、Q522I、Q522K、Q522M、Q522F、Q522W、Q522Y、Q522V和Q522L(表2)。六个G572变体在酸性pH 5.5下显示出相对于野生型HSA统计学上显著增加的FcRn/β2m结合：G572A、G572E、G572H、G572S、G572K和G572R(表3)。并未在pH 7.4下观测到任何HSA变体对FcRn/β2m的显著结合。在Q522L、A552V、G572R和K573Y的取代相对于野生型HSA在酸性pH5.5下显示出对FcRn/β2m结合最显著的增加(表4)。
实施例4：具有多个氨基酸取代的HSA变体的生成
为了测试突变对FcRn/β2m结合的累加或协同作用，如先前所述，生成具有双、三和四氨基酸取代的HSA变体。
如表5所示，双HSA变体Q522L/A552V、Q522L/G572R和A552V/G572R相对于野生型HSA和具有单一氨基酸取代的对应HSA变体在pH 5.5下显示出FcRn/β2m结合的显著改善。
携带K573Y突变的双HSA变体(Q522L/K573Y，A552V/K573Y和G572R/K573Y)相对于野生型HSA和单HSA变体Q522L、A552V、G572R在pH5.5下显示出FcRn/β2m结合的显著改善。双HSA变体Q552L/K573Y和A552V/K573Y而非G572R/K573Y相对于HSA变体K573Y在pH5.5下显示出FcRn/β2m结合的显著改善。
三HSA变体Q522L/A522V/G572R相对于野生型HSA和具有单一和双氨基酸取代的对应HSA变体在pH5.5下显示出显著改善的FcRn/β2m结合，并且结合水平大约是HSA变体K573Y的两倍(表5)。
三HSA变体Q522L/A552V/K573Y和Q522L/G572R/K573Y相对于野生型HSA和具有单一氨基酸取代的对应HSA变体在pH5.5下显示出显著改善的FcRn/β2m结合，以及相对于HSA变体K573Y显著改善的结合。
四HSA变体Q522L/A552V/G572R/K573Y相对于野生型HSA和具有单一氨基酸取代的对应HSA变体在pH5.5下显示出显著改善的FcRn/β2m结合。然而，该四变体相对于野生型HSA在pH7.4下还显示出显著增加的FcRn/β2m结合。
实施例5：具有单、双和三氨基酸取代的HSA变体的结合动力学
为了测试突变对FcRn/β2m结合的影响，如先前所述，生成了单、双和三HSA变体。使用具有BIAcoreTM 4000的SPR(GE医疗生命科学公司(GE Healthcare Life Sciences))测量结合动力学。重组hFcRn/β2M经化学生物素化并栓系于GE链霉亲和素传感器芯片(GE医疗生命科学公司)。简言之，使用以1：0.25摩尔比制备的扩展生物素接头(硫代-NHS-LC-LC-生物素)以较低的蛋白质：生物素比例在PBS中(即，最小的生物素化)对人FcRn/β2M进行化学修饰，在冰上2小时。根据生产商的说明，使用旋转柱(10000NMW)将反应混合物脱盐。
以5、1.7、0.6和0μM的浓度注射HSA变体。分析在10mM HEPES中进行；一式四份，150mM NaCl pH 6.0，37℃。监测结合和解离相100秒，各循环以中性pH 7.4下90秒的再生步骤结束。由各运行内的参比(斑点3)和空白缓冲液注射双重减去(double-subtract)传感图。
获得在pH 6下针对最小生物素化人FcRn筛选的所有HSA变体的速率常数和总体亲和力速率。获自1.7μM和0.6μM注射的数据与1：1结合模型良好拟合，而由5μM注射获得的数据由于饱和响应用于进行模型拟合。
如表6所示，八个Q522变体在酸性pH 6.0下显示出相对于野生型HSA增加的FcRn/β2m结合：Q522F、Q522G、Q522M、Q522K、Q522Y、Q522I、Q522A和Q522L。六个G572变体在酸性pH6.0下显示出相对于野生型HSA增加的FcRn/β2m结合：G572R、G572K、G572V、G572A、G572S和G572H(表6)。双HSA变体A522V/G572R、Q522L/A552V和三HSA变体Q522L/A552V/G572R在酸性pH 6.0下相对于野生型HSA都显示出增加的FcRn/β2m结合(表6)。
实施例6：具有单、双和三氨基酸取代的HSA变体的结合动力学
使用具有BIAcoreTM 4000的SPR(GE医疗生命科学公司)测量单、双和三HSA变体对FcRn/β2m结合的结合动力学。将HSA[H464Q]用作阴性对照。
重组hFcRn/β2M经化学生物素化并栓系于GE公司的链霉亲和素传感器芯片，如上所述。以2至0.015μM的浓度范围注射HSA变体。分析在10mM HEPES中进行；一式三份，150mMNaCl(pH 6.0)，37℃。监测结合相120秒，而解离相为240秒。各循环以在碱性条件(即，pH8.0)下90秒的再生步骤结束。由各运行内的参比和空白缓冲液注射双重减去传感图。
在酸性条件下获得的数据与1：1结合模型良好拟合。如先前所述建立速率常数和结合亲和力。
如表7所示，大部分HSA突变体相较于野生型HSA显示出结合亲和力(KD)的改善(高达3倍)。双HSA变体[Q522L/A552V]、[Q522L/G572R]和[A552V/G572R]相较于重组野生型HSA显示出对hFcRn/β2m高达10倍的结合亲和力改善。三HSA变体[Q522L/A552V/G572R]在大约25nM时具有最强的结合。阴性对照HSA[H464Q]不结合hFcRn/β2m。
实施例7：酸性和中性pH下选定的HSA变体对哺乳动物FcRn/β2m的结合亲和力
如先前所述生成单HSA变体G572R和K573Y、双HSA变体Q522L/A552V、Q522L/G572R和A552V/G572R和三HSA变体Q522L/A552V/G572R，并使用具有BIAcoreTM 4000的SPR(GE医疗生命科学公司)测量结合动力学。
将HSA变体稀释至1μg/mL并使用胺偶联化学(NHS/EDC)直接固定在羧甲基右旋糖酐(CM-5)传感器芯片(GE医疗生命科学公司)的两个表面上。HSA变体在各流通池的外部斑点(1和5)中固定为介于100至500RU的值，而在内部斑点(2和4)中固定为介于200至1000RU的值。各流通池的斑点3被激活/灭活并用于参比减法(reference subtraction)。FcRn/β2m的流速保持恒定在30μL/分钟。
在酸性(pH 6.0)和中性pH(pH7.3)下测试可溶性重组人、食蟹猴(“cyno”)、大鼠和小鼠FcRn/β2m与固定化的HSA变体的结合。使用2至0.007μM(pH6.0)和20至0.078μM(pH7.3)的浓度范围，并分别监测结合和解离相180秒和600秒。
如先前所述进行表面的再生。在酸性条件下获得的传感图数据与1：1结合模型良好拟合。然而，在pH 7.3下获得的传感图显示出接近仪器检测极限的解离速率，这需要稳态结合模型进行分析。
如表8所示，在pH 6.0下，人和cyno FcRn/β2m表现出纳摩尔结合亲和力。相较于野生型HSA，在pH 6下，人和cyno FcRn/β2m显示出对HSA K573Y的亲和力增加了将近20倍和对HSA G572R的亲和力增加了5倍。双HSA变体Q522L/A552V、Q522L/G572R和A552V/G572R对人FcRn/β2m的亲和力分别为约50nM、约27nM和约27nM，而对cyno FcRn/β2m的亲和力分别为约84nM、49nM和48nM。
与之相比，大鼠和鼠FcRn/β2m在相同条件下显示出弱结合至无结合。大鼠FcRn/β2m对HSA变体显示出弱100倍的亲和力，对野生型HSA、HSA变体Q522L/A552V和HSA变体G572R没有结合。在这些条件下，大鼠FcRn/β2m以大约1μM结合HSA K573Y，但是未检测到HSAG572R的结合。小鼠FcRn/β2m不结合任何测试的HSA变体。
如表8所示，在pH 7.3下，人和cyno FcRn/β2m不结合野生型HSA，并在pH7.3下显示出对HSA K573Y的弱结合(>50μM)。与其他HSA变体的结合亲和力范围为7至63μM。大鼠和鼠FcRn/β2m在pH 7.3下不结合任何测试的HSA变体。
实施例8：表达人FcRn的小鼠中HSA变体的药代动力学(PK)特性
为了测试HSA变体的PK特性，使用表达人FcRn受体的转基因小鼠(“hFcRn Tg32”纯合小鼠(即，B6.Cg-Fcgrttm1Dcr Tg(FCGRT)32Dcr/DcrJ)。性别和年龄混合的动物(10-14周龄；各时间点3只动物)静脉内注射10mg/kg的野生型HSA、单HSA变体K573Y、双HSA变体Q522L/A552V或三HSA变体Q522L/A552V/G572R。
收集血液并根据生产商的说明使用人白蛋白ELISA试剂盒(Bethyl实验室(BethylLaboratories)，目录号E88-129)评估人血清白蛋白的血浆水平，不同之处在于使用各测试物生成单独的参考曲线。分析之前，将数据针对各时间点取平均值，并使用定制MATLAB程序NCAPKfit通过非线性(Marquandt-Levenberg)最小化拟合对数据进行分析。使用最小二乘方藉由1/Y^2加权拟合完成模型拟合，并使用下述方程式为：
PK2(t)＝A*exp(-log(2)*t/T1)+B*exp(-log(2)*t/T2)。
使用标准统计学公式计算平均驻留时间(MRT)，曲线下面积(AUC)和清除速率。
如图1、表9和表10所示，野生型HSA的药代动力学特性与所有这三种HSA变体都显著不同，其中野生型HSA具有较短的平均驻留时间(MRT)、较小的曲线下面积(AUC)，和更快的清除。相较于野生型HSA，单HSA变体K573Y、双HSA变体Q522L/A552V和三HSA变体Q522L/A552V/G572R在所有三个标准(即MRT、AUC和清除)上均具有显著更好的药代动力学。
序列表
<110> CSL有限公司（CSL Limited）
<120> 人血清白蛋白变体及其应用
<130> 524788PCT
<150> AU 2017904211
<151> 2017-10-18
<160> 6
<170> PatentIn version 3.5
<210> 1
<211> 585
<212> PRT
<213> 智人（Homo sapiens）
<400> 1
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Ser Phe Phe Lys Met Leu Phe Leu Pro Glu Ser Ala Arg Trp Ile
1115 1120 1125
Gln Arg Thr His Gly Lys Asn Ser Leu Asn Ser Gly Gln Gly Pro
1130 1135 1140
Ser Pro Lys Gln Leu Val Ser Leu Gly Pro Glu Lys Ser Val Glu
1145 1150 1155
Gly Gln Asn Phe Leu Ser Glu Lys Asn Lys Val Val Val Gly Lys
1160 1165 1170
Gly Glu Phe Thr Lys Asp Val Gly Leu Lys Glu Met Val Phe Pro
1175 1180 1185
Ser Ser Arg Asn Leu Phe Leu Thr Asn Leu Asp Asn Leu His Glu
1190 1195 1200
Asn Asn Thr His Asn Gln Glu Lys Lys Ile Gln Glu Glu Ile Glu
1205 1210 1215
Lys Lys Glu Thr Leu Ile Gln Glu Asn Val Val Leu Pro Gln Ile
1220 1225 1230
His Thr Val Thr Gly Thr Lys Asn Phe Met Lys Asn Leu Phe Leu
1235 1240 1245
Leu Ser Thr Arg Gln Asn Val Glu Gly Ser Tyr Asp Gly Ala Tyr
1250 1255 1260
Ala Pro Val Leu Gln Asp Phe Arg Ser Leu Asn Asp Ser Thr Asn
1265 1270 1275
Arg Thr Lys Lys His Thr Ala His Phe Ser Lys Lys Gly Glu Glu
1280 1285 1290
Glu Asn Leu Glu Gly Leu Gly Asn Gln Thr Lys Gln Ile Val Glu
1295 1300 1305
Lys Tyr Ala Cys Thr Thr Arg Ile Ser Pro Asn Thr Ser Gln Gln
1310 1315 1320
Asn Phe Val Thr Gln Arg Ser Lys Arg Ala Leu Lys Gln Phe Arg
1325 1330 1335
Leu Pro Leu Glu Glu Thr Glu Leu Glu Lys Arg Ile Ile Val Asp
1340 1345 1350
Asp Thr Ser Thr Gln Trp Ser Lys Asn Met Lys His Leu Thr Pro
1355 1360 1365
Ser Thr Leu Thr Gln Ile Asp Tyr Asn Glu Lys Glu Lys Gly Ala
1370 1375 1380
Ile Thr Gln Ser Pro Leu Ser Asp Cys Leu Thr Arg Ser His Ser
1385 1390 1395
Ile Pro Gln Ala Asn Arg Ser Pro Leu Pro Ile Ala Lys Val Ser
1400 1405 1410
Ser Phe Pro Ser Ile Arg Pro Ile Tyr Leu Thr Arg Val Leu Phe
1415 1420 1425
Gln Asp Asn Ser Ser His Leu Pro Ala Ala Ser Tyr Arg Lys Lys
1430 1435 1440
Asp Ser Gly Val Gln Glu Ser Ser His Phe Leu Gln Gly Ala Lys
1445 1450 1455
Lys Asn Asn Leu Ser Leu Ala Ile Leu Thr Leu Glu Met Thr Gly
1460 1465 1470
Asp Gln Arg Glu Val Gly Ser Leu Gly Thr Ser Ala Thr Asn Ser
1475 1480 1485
Val Thr Tyr Lys Lys Val Glu Asn Thr Val Leu Pro Lys Pro Asp
1490 1495 1500
Leu Pro Lys Thr Ser Gly Lys Val Glu Leu Leu Pro Lys Val His
1505 1510 1515
Ile Tyr Gln Lys Asp Leu Phe Pro Thr Glu Thr Ser Asn Gly Ser
1520 1525 1530
Pro Gly His Leu Asp Leu Val Glu Gly Ser Leu Leu Gln Gly Thr
1535 1540 1545
Glu Gly Ala Ile Lys Trp Asn Glu Ala Asn Arg Pro Gly Lys Val
1550 1555 1560
Pro Phe Leu Arg Val Ala Thr Glu Ser Ser Ala Lys Thr Pro Ser
1565 1570 1575
Lys Leu Leu Asp Pro Leu Ala Trp Asp Asn His Tyr Gly Thr Gln
1580 1585 1590
Ile Pro Lys Glu Glu Trp Lys Ser Gln Glu Lys Ser Pro Glu Lys
1595 1600 1605
Thr Ala Phe Lys Lys Lys Asp Thr Ile Leu Ser Leu Asn Ala Cys
1610 1615 1620
Glu Ser Asn His Ala Ile Ala Ala Ile Asn Glu Gly Gln Asn Lys
1625 1630 1635
Pro Glu Ile Glu Val Thr Trp Ala Lys Gln Gly Arg Thr Glu Arg
1640 1645 1650
Leu Cys Ser Gln Asn Pro Pro Val Leu Lys Arg His Gln Arg Glu
1655 1660 1665
Ile Thr Arg Thr Thr Leu Gln Ser Asp Gln Glu Glu Ile Asp Tyr
1670 1675 1680
Asp Asp Thr Ile Ser Val Glu Met Lys Lys Glu Asp Phe Asp Ile
1685 1690 1695
Tyr Asp Glu Asp Glu Asn Gln Ser Pro Arg Ser Phe Gln Lys Lys
1700 1705 1710
Thr Arg His Tyr Phe Ile Ala Ala Val Glu Arg Leu Trp Asp Tyr
1715 1720 1725
Gly Met Ser Ser Ser Pro His Val Leu Arg Asn Arg Ala Gln Ser
1730 1735 1740
Gly Ser Val Pro Gln Phe Lys Lys Val Val Phe Gln Glu Phe Thr
1745 1750 1755
Asp Gly Ser Phe Thr Gln Pro Leu Tyr Arg Gly Glu Leu Asn Glu
1760 1765 1770
His Leu Gly Leu Leu Gly Pro Tyr Ile Arg Ala Glu Val Glu Asp
1775 1780 1785
Asn Ile Met Val Thr Phe Arg Asn Gln Ala Ser Arg Pro Tyr Ser
1790 1795 1800
Phe Tyr Ser Ser Leu Ile Ser Tyr Glu Glu Asp Gln Arg Gln Gly
1805 1810 1815
Ala Glu Pro Arg Lys Asn Phe Val Lys Pro Asn Glu Thr Lys Thr
1820 1825 1830
Tyr Phe Trp Lys Val Gln His His Met Ala Pro Thr Lys Asp Glu
1835 1840 1845
Phe Asp Cys Lys Ala Trp Ala Tyr Phe Ser Asp Val Asp Leu Glu
1850 1855 1860
Lys Asp Val His Ser Gly Leu Ile Gly Pro Leu Leu Val Cys His
1865 1870 1875
Thr Asn Thr Leu Asn Pro Ala His Gly Arg Gln Val Thr Val Gln
1880 1885 1890
Glu Phe Ala Leu Phe Phe Thr Ile Phe Asp Glu Thr Lys Ser Trp
1895 1900 1905
Tyr Phe Thr Glu Asn Met Glu Arg Asn Cys Arg Ala Pro Cys Asn
1910 1915 1920
Ile Gln Met Glu Asp Pro Thr Phe Lys Glu Asn Tyr Arg Phe His
1925 1930 1935
Ala Ile Asn Gly Tyr Ile Met Asp Thr Leu Pro Gly Leu Val Met
1940 1945 1950
Ala Gln Asp Gln Arg Ile Arg Trp Tyr Leu Leu Ser Met Gly Ser
1955 1960 1965
Asn Glu Asn Ile His Ser Ile His Phe Ser Gly His Val Phe Thr
1970 1975 1980
Val Arg Lys Lys Glu Glu Tyr Lys Met Ala Leu Tyr Asn Leu Tyr
1985 1990 1995
Pro Gly Val Phe Glu Thr Val Glu Met Leu Pro Ser Lys Ala Gly
2000 2005 2010
Ile Trp Arg Val Glu Cys Leu Ile Gly Glu His Leu His Ala Gly
2015 2020 2025
Met Ser Thr Leu Phe Leu Val Tyr Ser Asn Lys Cys Gln Thr Pro
2030 2035 2040
Leu Gly Met Ala Ser Gly His Ile Arg Asp Phe Gln Ile Thr Ala
2045 2050 2055
Ser Gly Gln Tyr Gly Gln Trp Ala Pro Lys Leu Ala Arg Leu His
2060 2065 2070
Tyr Ser Gly Ser Ile Asn Ala Trp Ser Thr Lys Glu Pro Phe Ser
2075 2080 2085
Trp Ile Lys Val Asp Leu Leu Ala Pro Met Ile Ile His Gly Ile
2090 2095 2100
Lys Thr Gln Gly Ala Arg Gln Lys Phe Ser Ser Leu Tyr Ile Ser
2105 2110 2115
Gln Phe Ile Ile Met Tyr Ser Leu Asp Gly Lys Lys Trp Gln Thr
2120 2125 2130
Tyr Arg Gly Asn Ser Thr Gly Thr Leu Met Val Phe Phe Gly Asn
2135 2140 2145
Val Asp Ser Ser Gly Ile Lys His Asn Ile Phe Asn Pro Pro Ile
2150 2155 2160
Ile Ala Arg Tyr Ile Arg Leu His Pro Thr His Tyr Ser Ile Arg
2165 2170 2175
Ser Thr Leu Arg Met Glu Leu Met Gly Cys Asp Leu Asn Ser Cys
2180 2185 2190
Ser Met Pro Leu Gly Met Glu Ser Lys Ala Ile Ser Asp Ala Gln
2195 2200 2205
Ile Thr Ala Ser Ser Tyr Phe Thr Asn Met Phe Ala Thr Trp Ser
2210 2215 2220
Pro Ser Lys Ala Arg Leu His Leu Gln Gly Arg Ser Asn Ala Trp
2225 2230 2235
Arg Pro Gln Val Asn Asn Pro Lys Glu Trp Leu Gln Val Asp Phe
2240 2245 2250
Gln Lys Thr Met Lys Val Thr Gly Val Thr Thr Gln Gly Val Lys
2255 2260 2265
Ser Leu Leu Thr Ser Met Tyr Val Lys Glu Phe Leu Ile Ser Ser
2270 2275 2280
Ser Gln Asp Gly His Gln Trp Thr Leu Phe Phe Gln Asn Gly Lys
2285 2290 2295
Val Lys Val Phe Gln Gly Asn Gln Asp Ser Phe Thr Pro Val Val
2300 2305 2310
Asn Ser Leu Asp Pro Pro Leu Leu Thr Arg Tyr Leu Arg Ile His
2315 2320 2325
Pro Gln Ser Trp Val His Gln Ile Ala Leu Arg Met
2330 2335 2340
<210> 3
<211> 462
<212> PRT
<213> 智人
<400> 3
Met Gln Arg Val Asn Met Ile Met Ala Glu Ser Pro Ser Leu Ile Thr
1 5 10 15
Ile Cys Leu Leu Gly Tyr Leu Leu Ser Ala Glu Cys Thr Val Phe Leu
20 25 30
Asp His Glu Asn Ala Asn Lys Ile Leu Asn Arg Pro Lys Arg Tyr Asn
35 40 45
Ser Gly Lys Leu Glu Glu Phe Val Gln Gly Asn Leu Glu Arg Glu Cys
50 55 60
Met Glu Glu Lys Cys Ser Phe Glu Glu Pro Arg Glu Val Phe Glu Asn
65 70 75 80
Thr Glu Lys Thr Thr Glu Phe Trp Lys Gln Tyr Val Asp Gly Asp Gln
85 90 95
Cys Glu Ser Asn Pro Cys Leu Asn Gly Gly Ser Cys Lys Asp Asp Ile
100 105 110
Asn Ser Tyr Glu Cys Trp Cys Pro Phe Gly Phe Glu Gly Lys Asn Cys
115 120 125
Glu Leu Asp Val Thr Cys Asn Ile Lys Asn Gly Arg Cys Glu Gln Phe
130 135 140
Cys Lys Asn Ser Ala Asp Asn Lys Val Val Cys Ser Cys Thr Glu Gly
145 150 155 160
Tyr Arg Leu Ala Glu Asn Gln Lys Ser Cys Glu Pro Ala Val Pro Phe
165 170 175
Pro Cys Gly Arg Val Ser Val Ser Gln Thr Ser Lys Leu Thr Arg Ala
180 185 190
Glu Ala Val Phe Pro Asp Val Asp Tyr Val Asn Pro Thr Glu Ala Glu
195 200 205
Thr Ile Leu Asp Asn Ile Thr Gln Gly Thr Gln Ser Phe Asn Asp Phe
210 215 220
Thr Arg Val Val Gly Gly Glu Asp Ala Lys Pro Gly Gln Phe Pro Trp
225 230 235 240
Gln Val Val Leu Asn Gly Lys Val Asp Ala Phe Cys Gly Gly Ser Ile
245 250 255
Val Asn Glu Lys Trp Ile Val Thr Ala Ala His Cys Val Glu Thr Gly
260 265 270
Val Lys Ile Thr Val Val Ala Gly Glu His Asn Ile Glu Glu Thr Glu
275 280 285
His Thr Glu Gln Lys Arg Asn Val Ile Arg Ala Ile Ile Pro His His
290 295 300
Asn Tyr Asn Ala Ala Ile Asn Lys Tyr Asn His Asp Ile Ala Leu Leu
305 310 315 320
Glu Leu Asp Glu Pro Leu Val Leu Asn Ser Tyr Val Thr Pro Ile Cys
325 330 335
Ile Ala Asp Lys Glu Tyr Thr Asn Ile Phe Leu Lys Phe Gly Ser Gly
340 345 350
Tyr Val Ser Gly Trp Ala Arg Val Phe His Lys Gly Arg Ser Ala Leu
355 360 365
Val Leu Gln Tyr Leu Arg Val Pro Leu Val Asp Arg Ala Thr Cys Leu
370 375 380
Arg Ser Thr Lys Phe Thr Ile Tyr Asn Asn Met Phe Cys Ala Gly Phe
385 390 395 400
His Glu Gly Gly Arg Asp Ser Cys Gln Gly Asp Ser Gly Gly Pro His
405 410 415
Val Thr Glu Val Glu Gly Thr Ser Phe Leu Thr Gly Ile Ile Ser Trp
420 425 430
Gly Glu Glu Cys Ala Met Lys Gly Lys Tyr Gly Ile Tyr Thr Lys Val
435 440 445
Ser Arg Tyr Val Asn Trp Ile Lys Glu Lys Thr Lys Leu Thr
450 455 460
<210> 4
<211> 488
<212> PRT
<213> 智人
<400> 4
Met Gly Arg Pro Leu His Leu Val Leu Leu Ser Ala Ser Leu Ala Gly
1 5 10 15
Leu Leu Leu Leu Gly Glu Ser Leu Phe Ile Arg Arg Glu Gln Ala Asn
20 25 30
Asn Ile Leu Ala Arg Val Thr Arg Ala Asn Ser Phe Leu Glu Glu Met
35 40 45
Lys Lys Gly His Leu Glu Arg Glu Cys Met Glu Glu Thr Cys Ser Tyr
50 55 60
Glu Glu Ala Arg Glu Val Phe Glu Asp Ser Asp Lys Thr Asn Glu Phe
65 70 75 80
Trp Asn Lys Tyr Lys Asp Gly Asp Gln Cys Glu Thr Ser Pro Cys Gln
85 90 95
Asn Gln Gly Lys Cys Lys Asp Gly Leu Gly Glu Tyr Thr Cys Thr Cys
100 105 110
Leu Glu Gly Phe Glu Gly Lys Asn Cys Glu Leu Phe Thr Arg Lys Leu
115 120 125
Cys Ser Leu Asp Asn Gly Asp Cys Asp Gln Phe Cys His Glu Glu Gln
130 135 140
Asn Ser Val Val Cys Ser Cys Ala Arg Gly Tyr Thr Leu Ala Asp Asn
145 150 155 160
Gly Lys Ala Cys Ile Pro Thr Gly Pro Tyr Pro Cys Gly Lys Gln Thr
165 170 175
Leu Glu Arg Arg Lys Arg Ser Val Ala Gln Ala Thr Ser Ser Ser Gly
180 185 190
Glu Ala Pro Asp Ser Ile Thr Trp Lys Pro Tyr Asp Ala Ala Asp Leu
195 200 205
Asp Pro Thr Glu Asn Pro Phe Asp Leu Leu Asp Phe Asn Gln Thr Gln
210 215 220
Pro Glu Arg Gly Asp Asn Asn Leu Thr Arg Ile Val Gly Gly Gln Glu
225 230 235 240
Cys Lys Asp Gly Glu Cys Pro Trp Gln Ala Leu Leu Ile Asn Glu Glu
245 250 255
Asn Glu Gly Phe Cys Gly Gly Thr Ile Leu Ser Glu Phe Tyr Ile Leu
260 265 270
Thr Ala Ala His Cys Leu Tyr Gln Ala Lys Arg Phe Lys Val Arg Val
275 280 285
Gly Asp Arg Asn Thr Glu Gln Glu Glu Gly Gly Glu Ala Val His Glu
290 295 300
Val Glu Val Val Ile Lys His Asn Arg Phe Thr Lys Glu Thr Tyr Asp
305 310 315 320
Phe Asp Ile Ala Val Leu Arg Leu Lys Thr Pro Ile Thr Phe Arg Met
325 330 335
Asn Val Ala Pro Ala Cys Leu Pro Glu Arg Asp Trp Ala Glu Ser Thr
340 345 350
Leu Met Thr Gln Lys Thr Gly Ile Val Ser Gly Phe Gly Arg Thr His
355 360 365
Glu Lys Gly Arg Gln Ser Thr Arg Leu Lys Met Leu Glu Val Pro Tyr
370 375 380
Val Asp Arg Asn Ser Cys Lys Leu Ser Ser Ser Phe Ile Ile Thr Gln
385 390 395 400
Asn Met Phe Cys Ala Gly Tyr Asp Thr Lys Gln Glu Asp Ala Cys Gln
405 410 415
Gly Asp Ser Gly Gly Pro His Val Thr Arg Phe Lys Asp Thr Tyr Phe
420 425 430
Val Thr Gly Ile Val Ser Trp Gly Glu Gly Cys Ala Arg Lys Gly Lys
435 440 445
Tyr Gly Ile Tyr Thr Lys Val Thr Ala Phe Leu Lys Trp Ile Asp Arg
450 455 460
Ser Met Lys Thr Arg Gly Leu Pro Lys Ala Lys Ser His Ala Pro Glu
465 470 475 480
Val Ile Thr Ser Ser Pro Leu Lys
485
<210> 5
<211> 466
<212> PRT
<213> 智人
<400> 5
Met Val Ser Gln Ala Leu Arg Leu Leu Cys Leu Leu Leu Gly Leu Gln
1 5 10 15
Gly Cys Leu Ala Ala Gly Gly Val Ala Lys Ala Ser Gly Gly Glu Thr
20 25 30
Arg Asp Met Pro Trp Lys Pro Gly Pro His Arg Val Phe Val Thr Gln
35 40 45
Glu Glu Ala His Gly Val Leu His Arg Arg Arg Arg Ala Asn Ala Phe
50 55 60
Leu Glu Glu Leu Arg Pro Gly Ser Leu Glu Arg Glu Cys Lys Glu Glu
65 70 75 80
Gln Cys Ser Phe Glu Glu Ala Arg Glu Ile Phe Lys Asp Ala Glu Arg
85 90 95
Thr Lys Leu Phe Trp Ile Ser Tyr Ser Asp Gly Asp Gln Cys Ala Ser
100 105 110
Ser Pro Cys Gln Asn Gly Gly Ser Cys Lys Asp Gln Leu Gln Ser Tyr
115 120 125
Ile Cys Phe Cys Leu Pro Ala Phe Glu Gly Arg Asn Cys Glu Thr His
130 135 140
Lys Asp Asp Gln Leu Ile Cys Val Asn Glu Asn Gly Gly Cys Glu Gln
145 150 155 160
Tyr Cys Ser Asp His Thr Gly Thr Lys Arg Ser Cys Arg Cys His Glu
165 170 175
Gly Tyr Ser Leu Leu Ala Asp Gly Val Ser Cys Thr Pro Thr Val Glu
180 185 190
Tyr Pro Cys Gly Lys Ile Pro Ile Leu Glu Lys Arg Asn Ala Ser Lys
195 200 205
Pro Gln Gly Arg Ile Val Gly Gly Lys Val Cys Pro Lys Gly Glu Cys
210 215 220
Pro Trp Gln Val Leu Leu Leu Val Asn Gly Ala Gln Leu Cys Gly Gly
225 230 235 240
Thr Leu Ile Asn Thr Ile Trp Val Val Ser Ala Ala His Cys Phe Asp
245 250 255
Lys Ile Lys Asn Trp Arg Asn Leu Ile Ala Val Leu Gly Glu His Asp
260 265 270
Leu Ser Glu His Asp Gly Asp Glu Gln Ser Arg Arg Val Ala Gln Val
275 280 285
Ile Ile Pro Ser Thr Tyr Val Pro Gly Thr Thr Asn His Asp Ile Ala
290 295 300
Leu Leu Arg Leu His Gln Pro Val Val Leu Thr Asp His Val Val Pro
305 310 315 320
Leu Cys Leu Pro Glu Arg Thr Phe Ser Glu Arg Thr Leu Ala Phe Val
325 330 335
Arg Phe Ser Leu Val Ser Gly Trp Gly Gln Leu Leu Asp Arg Gly Ala
340 345 350
Thr Ala Leu Glu Leu Met Val Leu Asn Val Pro Arg Leu Met Thr Gln
355 360 365
Asp Cys Leu Gln Gln Ser Arg Lys Val Gly Asp Ser Pro Asn Ile Thr
370 375 380
Glu Tyr Met Phe Cys Ala Gly Tyr Ser Asp Gly Ser Lys Asp Ser Cys
385 390 395 400
Lys Gly Asp Ser Gly Gly Pro His Ala Thr His Tyr Arg Gly Thr Trp
405 410 415
Tyr Leu Thr Gly Ile Val Ser Trp Gly Gln Gly Cys Ala Thr Val Gly
420 425 430
His Phe Gly Val Tyr Thr Arg Val Ser Gln Tyr Ile Glu Trp Leu Gln
435 440 445
Lys Leu Met Arg Ser Glu Pro Arg Pro Gly Val Leu Leu Arg Ala Pro
450 455 460
Phe Pro
465
<210> 6
<211> 2813
<212> PRT
<213> 智人
<400> 6
Met Ile Pro Ala Arg Phe Ala Gly Val Leu Leu Ala Leu Ala Leu Ile
1 5 10 15
Leu Pro Gly Thr Leu Cys Ala Glu Gly Thr Arg Gly Arg Ser Ser Thr
20 25 30
Ala Arg Cys Ser Leu Phe Gly Ser Asp Phe Val Asn Thr Phe Asp Gly
35 40 45
Ser Met Tyr Ser Phe Ala Gly Tyr Cys Ser Tyr Leu Leu Ala Gly Gly
50 55 60
Cys Gln Lys Arg Ser Phe Ser Ile Ile Gly Asp Phe Gln Asn Gly Lys
65 70 75 80
Arg Val Ser Leu Ser Val Tyr Leu Gly Glu Phe Phe Asp Ile His Leu
85 90 95
Phe Val Asn Gly Thr Val Thr Gln Gly Asp Gln Arg Val Ser Met Pro
100 105 110
Tyr Ala Ser Lys Gly Leu Tyr Leu Glu Thr Glu Ala Gly Tyr Tyr Lys
115 120 125
Leu Ser Gly Glu Ala Tyr Gly Phe Val Ala Arg Ile Asp Gly Ser Gly
130 135 140
Asn Phe Gln Val Leu Leu Ser Asp Arg Tyr Phe Asn Lys Thr Cys Gly
145 150 155 160
Leu Cys Gly Asn Phe Asn Ile Phe Ala Glu Asp Asp Phe Met Thr Gln
165 170 175
Glu Gly Thr Leu Thr Ser Asp Pro Tyr Asp Phe Ala Asn Ser Trp Ala
180 185 190
Leu Ser Ser Gly Glu Gln Trp Cys Glu Arg Ala Ser Pro Pro Ser Ser
195 200 205
Ser Cys Asn Ile Ser Ser Gly Glu Met Gln Lys Gly Leu Trp Glu Gln
210 215 220
Cys Gln Leu Leu Lys Ser Thr Ser Val Phe Ala Arg Cys His Pro Leu
225 230 235 240
Val Asp Pro Glu Pro Phe Val Ala Leu Cys Glu Lys Thr Leu Cys Glu
245 250 255
Cys Ala Gly Gly Leu Glu Cys Ala Cys Pro Ala Leu Leu Glu Tyr Ala
260 265 270
Arg Thr Cys Ala Gln Glu Gly Met Val Leu Tyr Gly Trp Thr Asp His
275 280 285
Ser Ala Cys Ser Pro Val Cys Pro Ala Gly Met Glu Tyr Arg Gln Cys
290 295 300
Val Ser Pro Cys Ala Arg Thr Cys Gln Ser Leu His Ile Asn Glu Met
305 310 315 320
Cys Gln Glu Arg Cys Val Asp Gly Cys Ser Cys Pro Glu Gly Gln Leu
325 330 335
Leu Asp Glu Gly Leu Cys Val Glu Ser Thr Glu Cys Pro Cys Val His
340 345 350
Ser Gly Lys Arg Tyr Pro Pro Gly Thr Ser Leu Ser Arg Asp Cys Asn
355 360 365
Thr Cys Ile Cys Arg Asn Ser Gln Trp Ile Cys Ser Asn Glu Glu Cys
370 375 380
Pro Gly Glu Cys Leu Val Thr Gly Gln Ser His Phe Lys Ser Phe Asp
385 390 395 400
Asn Arg Tyr Phe Thr Phe Ser Gly Ile Cys Gln Tyr Leu Leu Ala Arg
405 410 415
Asp Cys Gln Asp His Ser Phe Ser Ile Val Ile Glu Thr Val Gln Cys
420 425 430
Ala Asp Asp Arg Asp Ala Val Cys Thr Arg Ser Val Thr Val Arg Leu
435 440 445
Pro Gly Leu His Asn Ser Leu Val Lys Leu Lys His Gly Ala Gly Val
450 455 460
Ala Met Asp Gly Gln Asp Val Gln Leu Pro Leu Leu Lys Gly Asp Leu
465 470 475 480
Arg Ile Gln His Thr Val Thr Ala Ser Val Arg Leu Ser Tyr Gly Glu
485 490 495
Asp Leu Gln Met Asp Trp Asp Gly Arg Gly Arg Leu Leu Val Lys Leu
500 505 510
Ser Pro Val Tyr Ala Gly Lys Thr Cys Gly Leu Cys Gly Asn Tyr Asn
515 520 525
Gly Asn Gln Gly Asp Asp Phe Leu Thr Pro Ser Gly Leu Ala Glu Pro
530 535 540
Arg Val Glu Asp Phe Gly Asn Ala Trp Lys Leu His Gly Asp Cys Gln
545 550 555 560
Asp Leu Gln Lys Gln His Ser Asp Pro Cys Ala Leu Asn Pro Arg Met
565 570 575
Thr Arg Phe Ser Glu Glu Ala Cys Ala Val Leu Thr Ser Pro Thr Phe
580 585 590
Glu Ala Cys His Arg Ala Val Ser Pro Leu Pro Tyr Leu Arg Asn Cys
595 600 605
Arg Tyr Asp Val Cys Ser Cys Ser Asp Gly Arg Glu Cys Leu Cys Gly
610 615 620
Ala Leu Ala Ser Tyr Ala Ala Ala Cys Ala Gly Arg Gly Val Arg Val
625 630 635 640
Ala Trp Arg Glu Pro Gly Arg Cys Glu Leu Asn Cys Pro Lys Gly Gln
645 650 655
Val Tyr Leu Gln Cys Gly Thr Pro Cys Asn Leu Thr Cys Arg Ser Leu
660 665 670
Ser Tyr Pro Asp Glu Glu Cys Asn Glu Ala Cys Leu Glu Gly Cys Phe
675 680 685
Cys Pro Pro Gly Leu Tyr Met Asp Glu Arg Gly Asp Cys Val Pro Lys
690 695 700
Ala Gln Cys Pro Cys Tyr Tyr Asp Gly Glu Ile Phe Gln Pro Glu Asp
705 710 715 720
Ile Phe Ser Asp His His Thr Met Cys Tyr Cys Glu Asp Gly Phe Met
725 730 735
His Cys Thr Met Ser Gly Val Pro Gly Ser Leu Leu Pro Asp Ala Val
740 745 750
Leu Ser Ser Pro Leu Ser His Arg Ser Lys Arg Ser Leu Ser Cys Arg
755 760 765
Pro Pro Met Val Lys Leu Val Cys Pro Ala Asp Asn Leu Arg Ala Glu
770 775 780
Gly Leu Glu Cys Thr Lys Thr Cys Gln Asn Tyr Asp Leu Glu Cys Met
785 790 795 800
Ser Met Gly Cys Val Ser Gly Cys Leu Cys Pro Pro Gly Met Val Arg
805 810 815
His Glu Asn Arg Cys Val Ala Leu Glu Arg Cys Pro Cys Phe His Gln
820 825 830
Gly Lys Glu Tyr Ala Pro Gly Glu Thr Val Lys Ile Gly Cys Asn Thr
835 840 845
Cys Val Cys Arg Asp Arg Lys Trp Asn Cys Thr Asp His Val Cys Asp
850 855 860
Ala Thr Cys Ser Thr Ile Gly Met Ala His Tyr Leu Thr Phe Asp Gly
865 870 875 880
Leu Lys Tyr Leu Phe Pro Gly Glu Cys Gln Tyr Val Leu Val Gln Asp
885 890 895
Tyr Cys Gly Ser Asn Pro Gly Thr Phe Arg Ile Leu Val Gly Asn Lys
900 905 910
Gly Cys Ser His Pro Ser Val Lys Cys Lys Lys Arg Val Thr Ile Leu
915 920 925
Val Glu Gly Gly Glu Ile Glu Leu Phe Asp Gly Glu Val Asn Val Lys
930 935 940
Arg Pro Met Lys Asp Glu Thr His Phe Glu Val Val Glu Ser Gly Arg
945 950 955 960
Tyr Ile Ile Leu Leu Leu Gly Lys Ala Leu Ser Val Val Trp Asp Arg
965 970 975
His Leu Ser Ile Ser Val Val Leu Lys Gln Thr Tyr Gln Glu Lys Val
980 985 990
Cys Gly Leu Cys Gly Asn Phe Asp Gly Ile Gln Asn Asn Asp Leu Thr
995 1000 1005
Ser Ser Asn Leu Gln Val Glu Glu Asp Pro Val Asp Phe Gly Asn
1010 1015 1020
Ser Trp Lys Val Ser Ser Gln Cys Ala Asp Thr Arg Lys Val Pro
1025 1030 1035
Leu Asp Ser Ser Pro Ala Thr Cys His Asn Asn Ile Met Lys Gln
1040 1045 1050
Thr Met Val Asp Ser Ser Cys Arg Ile Leu Thr Ser Asp Val Phe
1055 1060 1065
Gln Asp Cys Asn Lys Leu Val Asp Pro Glu Pro Tyr Leu Asp Val
1070 1075 1080
Cys Ile Tyr Asp Thr Cys Ser Cys Glu Ser Ile Gly Asp Cys Ala
1085 1090 1095
Cys Phe Cys Asp Thr Ile Ala Ala Tyr Ala His Val Cys Ala Gln
1100 1105 1110
His Gly Lys Val Val Thr Trp Arg Thr Ala Thr Leu Cys Pro Gln
1115 1120 1125
Ser Cys Glu Glu Arg Asn Leu Arg Glu Asn Gly Tyr Glu Cys Glu
1130 1135 1140
Trp Arg Tyr Asn Ser Cys Ala Pro Ala Cys Gln Val Thr Cys Gln
1145 1150 1155
His Pro Glu Pro Leu Ala Cys Pro Val Gln Cys Val Glu Gly Cys
1160 1165 1170
His Ala His Cys Pro Pro Gly Lys Ile Leu Asp Glu Leu Leu Gln
1175 1180 1185
Thr Cys Val Asp Pro Glu Asp Cys Pro Val Cys Glu Val Ala Gly
1190 1195 1200
Arg Arg Phe Ala Ser Gly Lys Lys Val Thr Leu Asn Pro Ser Asp
1205 1210 1215
Pro Glu His Cys Gln Ile Cys His Cys Asp Val Val Asn Leu Thr
1220 1225 1230
Cys Glu Ala Cys Gln Glu Pro Gly Gly Leu Val Val Pro Pro Thr
1235 1240 1245
Asp Ala Pro Val Ser Pro Thr Thr Leu Tyr Val Glu Asp Ile Ser
1250 1255 1260
Glu Pro Pro Leu His Asp Phe Tyr Cys Ser Arg Leu Leu Asp Leu
1265 1270 1275
Val Phe Leu Leu Asp Gly Ser Ser Arg Leu Ser Glu Ala Glu Phe
1280 1285 1290
Glu Val Leu Lys Ala Phe Val Val Asp Met Met Glu Arg Leu Arg
1295 1300 1305
Ile Ser Gln Lys Trp Val Arg Val Ala Val Val Glu Tyr His Asp
1310 1315 1320
Gly Ser His Ala Tyr Ile Gly Leu Lys Asp Arg Lys Arg Pro Ser
1325 1330 1335
Glu Leu Arg Arg Ile Ala Ser Gln Val Lys Tyr Ala Gly Ser Gln
1340 1345 1350
Val Ala Ser Thr Ser Glu Val Leu Lys Tyr Thr Leu Phe Gln Ile
1355 1360 1365
Phe Ser Lys Ile Asp Arg Pro Glu Ala Ser Arg Ile Thr Leu Leu
1370 1375 1380
Leu Met Ala Ser Gln Glu Pro Gln Arg Met Ser Arg Asn Phe Val
1385 1390 1395
Arg Tyr Val Gln Gly Leu Lys Lys Lys Lys Val Ile Val Ile Pro
1400 1405 1410
Val Gly Ile Gly Pro His Ala Asn Leu Lys Gln Ile Arg Leu Ile
1415 1420 1425
Glu Lys Gln Ala Pro Glu Asn Lys Ala Phe Val Leu Ser Ser Val
1430 1435 1440
Asp Glu Leu Glu Gln Gln Arg Asp Glu Ile Val Ser Tyr Leu Cys
1445 1450 1455
Asp Leu Ala Pro Glu Ala Pro Pro Pro Thr Leu Pro Pro Asp Met
1460 1465 1470
Ala Gln Val Thr Val Gly Pro Gly Leu Leu Gly Val Ser Thr Leu
1475 1480 1485
Gly Pro Lys Arg Asn Ser Met Val Leu Asp Val Ala Phe Val Leu
1490 1495 1500
Glu Gly Ser Asp Lys Ile Gly Glu Ala Asp Phe Asn Arg Ser Lys
1505 1510 1515
Glu Phe Met Glu Glu Val Ile Gln Arg Met Asp Val Gly Gln Asp
1520 1525 1530
Ser Ile His Val Thr Val Leu Gln Tyr Ser Tyr Met Val Thr Val
1535 1540 1545
Glu Tyr Pro Phe Ser Glu Ala Gln Ser Lys Gly Asp Ile Leu Gln
1550 1555 1560
Arg Val Arg Glu Ile Arg Tyr Gln Gly Gly Asn Arg Thr Asn Thr
1565 1570 1575
Gly Leu Ala Leu Arg Tyr Leu Ser Asp His Ser Phe Leu Val Ser
1580 1585 1590
Gln Gly Asp Arg Glu Gln Ala Pro Asn Leu Val Tyr Met Val Thr
1595 1600 1605
Gly Asn Pro Ala Ser Asp Glu Ile Lys Arg Leu Pro Gly Asp Ile
1610 1615 1620
Gln Val Val Pro Ile Gly Val Gly Pro Asn Ala Asn Val Gln Glu
1625 1630 1635
Leu Glu Arg Ile Gly Trp Pro Asn Ala Pro Ile Leu Ile Gln Asp
1640 1645 1650
Phe Glu Thr Leu Pro Arg Glu Ala Pro Asp Leu Val Leu Gln Arg
1655 1660 1665
Cys Cys Ser Gly Glu Gly Leu Gln Ile Pro Thr Leu Ser Pro Ala
1670 1675 1680
Pro Asp Cys Ser Gln Pro Leu Asp Val Ile Leu Leu Leu Asp Gly
1685 1690 1695
Ser Ser Ser Phe Pro Ala Ser Tyr Phe Asp Glu Met Lys Ser Phe
1700 1705 1710
Ala Lys Ala Phe Ile Ser Lys Ala Asn Ile Gly Pro Arg Leu Thr
1715 1720 1725
Gln Val Ser Val Leu Gln Tyr Gly Ser Ile Thr Thr Ile Asp Val
1730 1735 1740
Pro Trp Asn Val Val Pro Glu Lys Ala His Leu Leu Ser Leu Val
1745 1750 1755
Asp Val Met Gln Arg Glu Gly Gly Pro Ser Gln Ile Gly Asp Ala
1760 1765 1770
Leu Gly Phe Ala Val Arg Tyr Leu Thr Ser Glu Met His Gly Ala
1775 1780 1785
Arg Pro Gly Ala Ser Lys Ala Val Val Ile Leu Val Thr Asp Val
1790 1795 1800
Ser Val Asp Ser Val Asp Ala Ala Ala Asp Ala Ala Arg Ser Asn
1805 1810 1815
Arg Val Thr Val Phe Pro Ile Gly Ile Gly Asp Arg Tyr Asp Ala
1820 1825 1830
Ala Gln Leu Arg Ile Leu Ala Gly Pro Ala Gly Asp Ser Asn Val
1835 1840 1845
Val Lys Leu Gln Arg Ile Glu Asp Leu Pro Thr Met Val Thr Leu
1850 1855 1860
Gly Asn Ser Phe Leu His Lys Leu Cys Ser Gly Phe Val Arg Ile
1865 1870 1875
Cys Met Asp Glu Asp Gly Asn Glu Lys Arg Pro Gly Asp Val Trp
1880 1885 1890
Thr Leu Pro Asp Gln Cys His Thr Val Thr Cys Gln Pro Asp Gly
1895 1900 1905
Gln Thr Leu Leu Lys Ser His Arg Val Asn Cys Asp Arg Gly Leu
1910 1915 1920
Arg Pro Ser Cys Pro Asn Ser Gln Ser Pro Val Lys Val Glu Glu
1925 1930 1935
Thr Cys Gly Cys Arg Trp Thr Cys Pro Cys Val Cys Thr Gly Ser
1940 1945 1950
Ser Thr Arg His Ile Val Thr Phe Asp Gly Gln Asn Phe Lys Leu
1955 1960 1965
Thr Gly Ser Cys Ser Tyr Val Leu Phe Gln Asn Lys Glu Gln Asp
1970 1975 1980
Leu Glu Val Ile Leu His Asn Gly Ala Cys Ser Pro Gly Ala Arg
1985 1990 1995
Gln Gly Cys Met Lys Ser Ile Glu Val Lys His Ser Ala Leu Ser
2000 2005 2010
Val Glu Leu His Ser Asp Met Glu Val Thr Val Asn Gly Arg Leu
2015 2020 2025
Val Ser Val Pro Tyr Val Gly Gly Asn Met Glu Val Asn Val Tyr
2030 2035 2040
Gly Ala Ile Met His Glu Val Arg Phe Asn His Leu Gly His Ile
2045 2050 2055
Phe Thr Phe Thr Pro Gln Asn Asn Glu Phe Gln Leu Gln Leu Ser
2060 2065 2070
Pro Lys Thr Phe Ala Ser Lys Thr Tyr Gly Leu Cys Gly Ile Cys
2075 2080 2085
Asp Glu Asn Gly Ala Asn Asp Phe Met Leu Arg Asp Gly Thr Val
2090 2095 2100
Thr Thr Asp Trp Lys Thr Leu Val Gln Glu Trp Thr Val Gln Arg
2105 2110 2115
Pro Gly Gln Thr Cys Gln Pro Ile Leu Glu Glu Gln Cys Leu Val
2120 2125 2130
Pro Asp Ser Ser His Cys Gln Val Leu Leu Leu Pro Leu Phe Ala
2135 2140 2145
Glu Cys His Lys Val Leu Ala Pro Ala Thr Phe Tyr Ala Ile Cys
2150 2155 2160
Gln Gln Asp Ser Cys His Gln Glu Gln Val Cys Glu Val Ile Ala
2165 2170 2175
Ser Tyr Ala His Leu Cys Arg Thr Asn Gly Val Cys Val Asp Trp
2180 2185 2190
Arg Thr Pro Asp Phe Cys Ala Met Ser Cys Pro Pro Ser Leu Val
2195 2200 2205
Tyr Asn His Cys Glu His Gly Cys Pro Arg His Cys Asp Gly Asn
2210 2215 2220
Val Ser Ser Cys Gly Asp His Pro Ser Glu Gly Cys Phe Cys Pro
2225 2230 2235
Pro Asp Lys Val Met Leu Glu Gly Ser Cys Val Pro Glu Glu Ala
2240 2245 2250
Cys Thr Gln Cys Ile Gly Glu Asp Gly Val Gln His Gln Phe Leu
2255 2260 2265
Glu Ala Trp Val Pro Asp His Gln Pro Cys Gln Ile Cys Thr Cys
2270 2275 2280
Leu Ser Gly Arg Lys Val Asn Cys Thr Thr Gln Pro Cys Pro Thr
2285 2290 2295
Ala Lys Ala Pro Thr Cys Gly Leu Cys Glu Val Ala Arg Leu Arg
2300 2305 2310
Gln Asn Ala Asp Gln Cys Cys Pro Glu Tyr Glu Cys Val Cys Asp
2315 2320 2325
Pro Val Ser Cys Asp Leu Pro Pro Val Pro His Cys Glu Arg Gly
2330 2335 2340
Leu Gln Pro Thr Leu Thr Asn Pro Gly Glu Cys Arg Pro Asn Phe
2345 2350 2355
Thr Cys Ala Cys Arg Lys Glu Glu Cys Lys Arg Val Ser Pro Pro
2360 2365 2370
Ser Cys Pro Pro His Arg Leu Pro Thr Leu Arg Lys Thr Gln Cys
2375 2380 2385
Cys Asp Glu Tyr Glu Cys Ala Cys Asn Cys Val Asn Ser Thr Val
2390 2395 2400
Ser Cys Pro Leu Gly Tyr Leu Ala Ser Thr Ala Thr Asn Asp Cys
2405 2410 2415
Gly Cys Thr Thr Thr Thr Cys Leu Pro Asp Lys Val Cys Val His
2420 2425 2430
Arg Ser Thr Ile Tyr Pro Val Gly Gln Phe Trp Glu Glu Gly Cys
2435 2440 2445
Asp Val Cys Thr Cys Thr Asp Met Glu Asp Ala Val Met Gly Leu
2450 2455 2460
Arg Val Ala Gln Cys Ser Gln Lys Pro Cys Glu Asp Ser Cys Arg
2465 2470 2475
Ser Gly Phe Thr Tyr Val Leu His Glu Gly Glu Cys Cys Gly Arg
2480 2485 2490
Cys Leu Pro Ser Ala Cys Glu Val Val Thr Gly Ser Pro Arg Gly
2495 2500 2505
Asp Ser Gln Ser Ser Trp Lys Ser Val Gly Ser Gln Trp Ala Ser
2510 2515 2520
Pro Glu Asn Pro Cys Leu Ile Asn Glu Cys Val Arg Val Lys Glu
2525 2530 2535
Glu Val Phe Ile Gln Gln Arg Asn Val Ser Cys Pro Gln Leu Glu
2540 2545 2550
Val Pro Val Cys Pro Ser Gly Phe Gln Leu Ser Cys Lys Thr Ser
2555 2560 2565
Ala Cys Cys Pro Ser Cys Arg Cys Glu Arg Met Glu Ala Cys Met
2570 2575 2580
Leu Asn Gly Thr Val Ile Gly Pro Gly Lys Thr Val Met Ile Asp
2585 2590 2595
Val Cys Thr Thr Cys Arg Cys Met Val Gln Val Gly Val Ile Ser
2600 2605 2610
Gly Phe Lys Leu Glu Cys Arg Lys Thr Thr Cys Asn Pro Cys Pro
2615 2620 2625
Leu Gly Tyr Lys Glu Glu Asn Asn Thr Gly Glu Cys Cys Gly Arg
2630 2635 2640
Cys Leu Pro Thr Ala Cys Thr Ile Gln Leu Arg Gly Gly Gln Ile
2645 2650 2655
Met Thr Leu Lys Arg Asp Glu Thr Leu Gln Asp Gly Cys Asp Thr
2660 2665 2670
His Phe Cys Lys Val Asn Glu Arg Gly Glu Tyr Phe Trp Glu Lys
2675 2680 2685
Arg Val Thr Gly Cys Pro Pro Phe Asp Glu His Lys Cys Leu Ala
2690 2695 2700
Glu Gly Gly Lys Ile Met Lys Ile Pro Gly Thr Cys Cys Asp Thr
2705 2710 2715
Cys Glu Glu Pro Glu Cys Asn Asp Ile Thr Ala Arg Leu Gln Tyr
2720 2725 2730
Val Lys Val Gly Ser Cys Lys Ser Glu Val Glu Val Asp Ile His
2735 2740 2745
Tyr Cys Gln Gly Lys Cys Ala Ser Lys Ala Met Tyr Ser Ile Asp
2750 2755 2760
Ile Asn Asp Val Gln Asp Gln Cys Ser Cys Cys Ser Pro Thr Arg
2765 2770 2775
Thr Glu Pro Met Gln Val Ala Leu His Cys Thr Asn Gly Ser Val
2780 2785 2790
Val Tyr His Glu Val Leu Asn Ala Met Glu Cys Lys Cys Ser Pro
2795 2800 2805
Arg Lys Cys Ser Lys
2810
Claims (28)
1.血清白蛋白变体或其功能片段，其包含选自下组的一种或多种氨基酸取代：
(i).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸；
(ii).缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸；
(iii).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸；和
(iv).其组合。
2.如权利要求1所述的血清白蛋白变体或其功能片段，其中，相较于SEQ ID NO:1中所示的血清白蛋白，所述血清白蛋白变体或其功能片段结合FcRn的亲和力增加。
3.如权利要求2所述的血清白蛋白变体或其功能片段，其中，所述结合亲和力在酸性pH下测量。
4.如权利要求1-3中任一项所述的血清白蛋白变体或其功能片段，其中，相较于SEQ IDNO:1中所示的血清白蛋白，所述血清白蛋白变体或其功能片段的血清半衰期增加。
5.如权利要求1-4中任一项所述的血清白蛋白变体或其功能片段，其包含：
(i).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，和缬氨酸取代SEQ ID NO:1位置552处的丙氨酸；或
(ii).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，和选自下组的氨基酸取代SEQ ID NO:1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸；或
(iii).缬氨酸取代对应SEQ ID NO：1氨基酸552的位置处的丙氨酸，和选自下组的氨基酸取代SEQ ID NO：1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸；或
(iv).选自下组的氨基酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺：甘氨酸，异亮氨酸，赖氨酸，甲硫氨酸，苯丙氨酸，色氨酸，酪氨酸，缬氨酸和亮氨酸，缬氨酸取代SEQ ID NO:1位置552处的丙氨酸，和选自下组的氨基酸取代SEQ ID NO:1位置572处的甘氨酸：丙氨酸，谷氨酸，组氨酸，丝氨酸，赖氨酸和精氨酸。
6.如权利要求1-5中任一项所述的血清白蛋白变体或其功能片段，其还包含酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
7.如权利要求1-6中任一项所述的血清白蛋白变体或其功能片段，其包含：
(i).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺；和/或
(ii).缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸；和/或
(iii).精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸。
8.如权利要求1-7中任一项所述的血清白蛋白变体或其功能片段，其包含：
(i).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，和精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸；或
(ii).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，和缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸；或
(iii).缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸；或
(iv).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(v).缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(vi).精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(vii).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸；或
(viii).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(ix).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸；或
(x).亮氨酸取代对应SEQ ID NO:1氨基酸522的位置处的谷氨酰胺，缬氨酸取代对应SEQ ID NO:1氨基酸552的位置处的丙氨酸，精氨酸取代对应SEQ ID NO:1氨基酸572的位置处的甘氨酸，和酪氨酸取代对应SEQ ID NO:1氨基酸573的位置处的赖氨酸。
9.一种血清白蛋白偶联物，其包含权利要求1-8中任一项所述的血清白蛋白变体或其功能片段以及化合物。
10.如权利要求9所述的血清白蛋白偶联物，其中血清白蛋白偶联物的血清半衰期相较于包含SEQ ID NO:1中所示血清白蛋白的血清白蛋白偶联物更长。
11.如权利要求9或10所述的血清白蛋白偶联物，其中血清白蛋白偶联物对FcRn的结合亲和力相较于包含SEQ ID NO:1中所示血清白蛋白的血清白蛋白偶联物增加。
12.如权利要求9至11中任一项所述的血清白蛋白偶联物，其中，所述化合物是蛋白质，含抗体可变区的蛋白质，抗体模拟物，结构域抗体，毒素，放射性同位素，可检测标记物，肽，多肽，胶体，化疗剂，核酸，小分子，反义寡核苷酸，短发夹RNA(shRNA)，siRNA，干扰RNA(RNAi)，核酶，微小RNA，微小RNA适应性shRNA(shRNAmir)，DNA酶及其混合物。
13.如权利要求12所述的血清白蛋白偶联物，其中，所述化合物是含Fv的蛋白质。
14.如权利要求13所述的血清白蛋白偶联物，其中，所述蛋白质选自下组：
(i).单链Fv片段(scFv)；
(ii).二聚体scFv(di-scFv)；或
(iii).双抗体；
(iv).三抗体；
(v).四抗体；
(vi).Fab；
(vii).F(ab’)2；
(viii).Fv；或
(ix).与抗体的恒定区、Fc或重链恒定结构域(CH)2和/或CH3相连的(i)-(viii)之一。
15.如权利要求12所述的血清白蛋白偶联物，其中，所述蛋白质是治疗性蛋白质。
16.如权利要求9-15中任一项所述的血清白蛋白偶联物，其中，所述化合物是血管性血友病因子或其修饰形式。
17.如权利要求16所述的血清白蛋白偶联物，其中，所述血管性血友病因子包含D′D3结构域。
18.如权利要求9-15中任一项所述的血清白蛋白偶联物，其中，所述化合物是补体抑制剂或其修饰形式。
19.如权利要求9-15中任一项所述的血清白蛋白偶联物，其中，所述化合物是或结合凝血因子。
20.如权利要求19所述的血清白蛋白偶联物，其中，所述凝血因子选自下组：因子I，因子II(凝血酶原)/凝血酶、因子III、因子V、因子VII、因子VIII、因子IX、因子X、因子XI、因子XII、因子XIII和前述任一者的活化形式。
21.一种组合物，其包含如权利要求9-20中任一项所述的血清白蛋白偶联物和药物运载体和/或赋形剂。
22.如权利要求1-8中任一项所述的血清白蛋白变体或其功能片段或如权利要求9-20中任一项所述的血清白蛋白偶联物，其用于治疗或预防对象中疾病或病症。
23.一种治疗或预防对象中疾病或病症的方法，所述方法包括给予如权利要求9-20中任一项所述的血清白蛋白偶联物或如权利要求21所述的组合物。
24.如权利要求9-20中任一项所述的血清白蛋白偶联物或如权利要求21所述的组合物在制备用于治疗或预防对象中疾病或病症的药物中的用途。
25.如权利要求22所述用途的血清白蛋白变体、偶联物或组合物，权利要求23所述的方法，或权利要求24所述的用途，其中，所述疾病或病症是出血性疾病。
26.如权利要求22或25所述用途的血清白蛋白变体、偶联物或组合物，权利要求23或25所述的方法，或权利要求24或25所述的用途，其中，所述对象处于发展出出血性疾病或其症状的风险中。
27.如权利要求22、25或26所述用途的血清白蛋白变体、偶联物或组合物，或如权利要求23、25或26中任一项所述的方法，或如权利要求24-26中任一项所述的用途，其中，所述出血性疾病是A型血友病、B型血友病、血管性血友病、因子I缺乏症、因子II缺乏症、因子V缺乏症、因子V/因子VIII组合型缺乏症、因子VII缺乏症、因子X缺乏症、因子XI缺乏症或因子XIII缺乏症。
28.一种用于治疗或预防对象中出血性疾病的试剂盒，所述试剂盒包括：
(a).至少一种如权利要求9-20中任一项所述的血清白蛋白偶联物或如权利要求21所述的组合物；
(b).关于使用所述试剂盒治疗或预防对象中出血性疾病的说明书；和
(c).任选地，至少一种其他治疗活性化合物或药物。
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- 2018-10-18 CA CA3072634A patent/CA3072634A1/en active Pending
- 2018-10-18 US US16/640,562 patent/US11466073B2/en active Active
- 2018-10-18 KR KR1020207011692A patent/KR20200067158A/ko not_active Application Discontinuation
- 2018-10-18 JP JP2020521872A patent/JP2020537668A/ja active Pending
- 2018-10-18 EP EP18869079.6A patent/EP3697812A4/en active Pending
- 2018-10-18 WO PCT/AU2018/051131 patent/WO2019075519A1/en unknown
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| JP2023099663A (ja) | 2023-07-13 |
| CN111247165B (zh) | 2023-11-10 |
| KR20200067158A (ko) | 2020-06-11 |
| AU2018350370A1 (en) | 2020-02-20 |
| US20230086472A1 (en) | 2023-03-23 |
| US20200325209A1 (en) | 2020-10-15 |
| EP3697812A4 (en) | 2021-09-22 |
| US11466073B2 (en) | 2022-10-11 |
| EP3697812A1 (en) | 2020-08-26 |
| CA3072634A1 (en) | 2019-04-25 |
| JP2020537668A (ja) | 2020-12-24 |
| WO2019075519A1 (en) | 2019-04-25 |
| AU2018350370B2 (en) | 2023-05-04 |
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