CN101565858A - 包含肽结合域的组合物及由其形成纳米颗粒和纳米导线的方法 - Google Patents
包含肽结合域的组合物及由其形成纳米颗粒和纳米导线的方法 Download PDFInfo
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Abstract
本发明涉及包括一种或多种肽结合域的组合物,所述结合域选择性地与无机靶晶体组合物结合或与无机靶晶体组合物的晶面结合,该结合域选择性地使靶晶体组合物的纳米颗粒成核。本发明还涉及由所述组合物形成纳米颗粒和纳米导线的方法。
Description
本申请为以下申请的分案申请:申请号为02821295.9、申请日为2002年9月27日、发明名称为纳米颗粒的生物控制。
技术领域
本发明涉及各种材料的选择性识别,尤其涉及使用有机聚合物对半导体材料和含碳材料的表面识别。
本申请要求2001年9月28日递交的序列号为No.60/325,664的临时专利申请的优先权。
本申请所进行的研究是部分由Army Research Office提供支持的(DADD19-99-0155)。
核苷酸和/或氨基酸序列表提供了计算机可读形式作为参考。
背景技术
在生物学系统中,有机分子对诸如碳酸钙和硅石等无机材料的晶核形成以及矿石相位具有显著的控制作用,同时对生物功能所需的复杂结构中微晶和其它纳米模块的组装也具有显著的作用。这种控制功能在理论上可以应用于具有特定磁学、电学或光学特性的材料上。
生物方法制备出的材料通常很柔软,它由分子模块(即,脂类、肽类、以及核酸)的极其简单的集合构成,而这些分子模块却具有非常复杂的排列结构。半导体工业需要依靠一系列光刻技术处理步骤从而在集成电路上构建最小的部件,而与此很不相同的是,活性生物体在大部分情况下利用共价和非共价力同时作用在许多分子组件上,以实现其结构。而且,这些结构通常能够在两个或多个可用构型之间进行精细的重排,而不改变任何分子组成。
利用“生物”材料来处理下一代微电子、光学和磁学设备能够为解决传统的处理方法中所存在的问题提供一种可能的解决方案。该处理方法中的关键性因素是确定生物一无机-有机材料合适的兼容性以及结合性、用于创建独特的和特异性结合的合成步骤及识别,以及理解恰当的模块的合成。
本发明概述
本发明是根据有机聚合物(例如肽)的选择、生产、分离和表征,这些聚合物对各种有机和无机材料具有高选择性。在本发明的一个实施方式中,生物材料,例如噬菌体展示文库的组合物库,利用多肽进化的多次反复来对靶物质进行直接的分子识别。可构建有机聚合物(例如肽),使其能与许多材料高特异性结合,这些材料包括但不限于半导体表面和例如碳纳米管和石墨的含碳元素的物质。此外,不管是否使用了结构类似材料的组合,本发明可以允许有机识别分子(例如,有机聚合物)的选择性分离,其中该有机识别分子能特异性识别生物材料的取向、形状或结构(例如,结晶形状或取向)。
在本发明的一个实施方式中公开了一种生物支架。该支架包括能结合一种或多种生物材料的基底,与基底结合的一种或多种生物材料,以及与生物材料结合的一种或多种含碳元素的分子。在本发明的另一个实施方式中,所公开的生物支架包含能结合一种或多种生物材料的基底,与基底结合的第一生物材料,与第一生物材料结合的第二生物材料,以及与第二生物材料结合的一种或多种含碳的分子。
在本发明的另一个实施方式中,该生物支架包括能结合一种或多种噬菌体的基底,与基底结合的一种或多种噬菌体,能识别噬菌体部分位置的一种或多种肽,以及能识别肽的一种或多种含碳的分子。
在本发明的另一个实施方式公开了一种制备生物支架的方法。该方法包括:提供一种能结合一种或多种生物材料的基底,将一种或多种生物材料与基底结合,并且将一种或多种含碳元素的分子与生物材料接触,形成生物支架。
本发明的另一个实施方式记载了一种分子。该分子包含一种能选择性识别含碳元素分子的有机聚合物。
本发明的另一个实施方式公开了一种受介导的半导体形成(directedsemiconductor formation)的方法。该方法包括:将与预先确定的表面特异性半导体材料结合的分子与第一种离子接触,来构建半导体材料前体物,往半导体材料前体物中加入第二种离子,其中所述的分子控制预先确定的表面特异性半导体材料的形成。该分子可以包括氨基酸寡聚物或肽,它们可在噬菌体的表面作为例如嵌合包被蛋白的一部分。该分子还可以是核酸寡聚物,并且可选自组合文库。该分子可以是约7-20个氨基酸的氨基酸聚合物。本发明还进一步包括利用本发明的方法制备得到的半导体材料。
使用本发明的材料和方法介导和生长的受控晶体的用途包括获得具有新型光学、电学和磁学特性的材料。正如本领域的技术人员所知,具体的光学、电学和磁学特性可以通过半导体晶体的形成来介导,例如通过使装置形成图样(patterning the devices)的过程来介导,本发明的图样形成可包括分层或底层图样的形成,从而构建具有图样、层状或两者都有的晶体形式。
本发明形成图样和/或分层的另一个用途是形成具有高密度磁性存储特性的半导体装置。另一种设计可能是用于例如量子计算中的晶体管形成。本发明的图样、设计和新材料的另一个用途包括医学应用中的成像和成像对照剂。
受介导的(directed)半导体和半导体晶体形成的一种用途包括基于量子点图样的信息存储,例如在军事或个人环境中分辩敌友。量子点能根据对织物、装甲或人的鉴定来区分单个的士兵或个人。另外,点还可用来编码钱币的质地。本发明的另一个用途是构建用于给药的双功能和多功能肽,它使用本发明的肽将要运输的药物进行包埋(trapping)。本发明的另一个用途是采用肽的药物包埋给药,根据基因或蛋白表达进行体内和体外诊断。
为了更完整地理解本发明的特征以及优点,现结合附图对本发明进行详细描述。
附图说明
为了更完整地理解本发明的特征以及优点,现结合附图对本发明进行详细描述。图1描述了根据本发明选择的随机氨基酸序列;
图2描述了本发明的XPS结构光谱;
图3描述了本发明的噬菌体识别异质结构;
图4-8描述了本发明的特定氨基酸序列;
图9为本发明噬菌体文库的肽插入结构;
图10为本发明的第三和第四次选择中的各种氨基酸取代;
图11为本发明的第五次选择后的氨基酸取代;
图12为本发明从ZnS纳米颗粒制得的纳米导线(nanowire);
图13为本发明针对碳模板(carbon planchet)选择PhD-C7C文库而获得的有机聚合物(例如肽)序列;
图14为本发明针对碳模板选择PhD-12文库而获得的有机聚合物(例如肽)序列;
图15为本发明针对SWNT导电胶聚集物(paste aggregate)选择PhD-12文库而获得的有机聚合物(例如肽)序列;
图16为本发明针对HOPG选择PhD-12文库而获得的有机聚合物(例如肽)序列;
图17为本发明的各种噬菌体克隆对SWNT导电胶聚集物的结合效率;
图18为本发明的各种噬菌体克隆与碳模板的结合效率;
图19为本发明的各种噬菌体克隆与碳模板结合的共聚焦成像;
图20为本发明的各种生物素化的肽与碳模板结合的共聚焦成像;
图21为本发明的各种噬菌体克隆与湿SWNT导电胶(paste)结合的共聚焦成像;
图22为本发明HOPG上的噬菌体克隆的AFM成像;
图23为SWNT纯化反向柱的示意图;
图24为噬菌体与SWNT结合(噬菌体-SWNT)的示意图;
图25为使用SWNT结合肽修饰n-型SWNT的示意图;
图26为SWNT用作药物释放系统的示意图;
图27为SWNT用作癌症药物的示意图;
本发明的详细描述
尽管本发明下面将对所使用的实施例进行详细讨论,应当了解本发明提供了许多使用的发明观念,这些观念可在多种特定环境下实施。本文所讨论的特定实施例仅仅阐述了制造和使用本发明的特定方式,而并非为了对本发明做出限制。
本发明所用的术语具有本领域普通技术人员通常理解的含义。在此所用的术语是为了描述特定的实施例,但不是用于限制本发明,除非出现在权利要求中。
本发明说明书中所用的术语是为了描述特定的实施例,但不是用于限制本发明,除非出现在权利要求中。本发明的说明书中,术语“量子点”、“纳米颗粒”和“颗粒”是可以互换的。
所用的术语“生物材料”和/或“生物材料”是指病毒、噬菌体、细菌、肽、蛋白、氨基酸、类固醇、药物、生色团、抗体、酶、单链或双链核酸、以及它们的任何化学修饰物。生物材料可在基底的接触表面自装配来形成干的薄膜。自装配允许生物材料在表面随机或均一排列。另外,生物材料形成的干薄膜受外界因素控制,例如溶剂浓度、加了电场和/或磁场、光学或其它化学或场相互作用。在这儿提到的术语生物材料、有机聚合物和聚合有机材料可以互换。在这儿用到的有机聚合物指多单元的有机材料,其中有机材料包含几个相同或不同的“单体”。有机聚合物的例子例如:存在于生物系统(例如真核生物)中的蛋白、抗体、肽、核酸、嵌合分子、药物和其它含碳材料。其它的有机聚合物可以是生物聚合物的衍生物或类似物,其中该生物聚合物包含一个或多个生物单体以及模拟天然功能的合成单体。
术语“无机分子”或“无机化合物”所指的化合物,例如铟锡氧化物、掺杂剂、金属、矿物、放射性同位素、盐,及其组合物。金属包括Ba,Sr,Ti,Bi,Ta,Zr,Fe,Ni,Mn,Pb,La,Li,Na,K,Rb,Cs,Fr,Be,Mg,Ca,Nb,Tl,Hg,Cu,Co,Rh,Sc,或Y。无机化合物包括,例如高介电常数材料(绝缘体)如钛酸锶钡、锆钛酸钡、锆钛酸铅、钛酸镧铅、钛酸锶、钛酸钡、氟化钡镁、钛酸铋、锶酸铋酸钽(strontium bismuth tantalite)和锶酸铋酸铌酸钽(strontiumbismuth tantalite niobate),或本领域普通技术人员所知的它们的变化体。
术语“有机分子”或“有机化合物”指含单独或组合的碳的化合物,例如核苷酸、多核苷酸、核苷、类固醇、DNA、RNA、肽、蛋白、抗体、酶、碳水化合物、脂、导电聚合物(conducting polymers)、药物,及其组合物。药物可包含抗生物素、抗菌剂、消炎剂、止痛剂、抗组胺药,以及用于哺乳动物病理(或潜在病理)条件下的任何治疗或预防剂。
术语“含元素碳的分子”一般指碳的同素异形体。具体的例子包括但不限于金刚石、石墨、活性碳、碳60、碳黑、工业碳、木炭、焦炭和钢。其它的例子包括但不限于碳模板、高度有序的热解石墨(HOPG)、单壁纳米管(SWNT)、单壁纳米管导电胶(single-walled nanotube paste)、多壁纳米管、多壁纳米管导电胶,以及加入金属的含碳材料。
在此提到的“基底”可以是微加工的固体表面,可通过共价或非共价键结合分子,基底包括例如硅、Langmuir-Bodgett膜、功能化玻璃、锗、陶瓷、硅、半导体材料、PTFE、碳、聚碳酸脂、云母、聚酯薄膜、塑料、石英、聚苯乙烯、砷化镓、金、银、金属、合金、织物,及其组合物且具有与表面结合的下述官能团,例如氨基、羧基、硫羟基(thiol)或羟基。类似地,基底可以是一种有机材料,例如蛋白、哺乳动物细胞、抗体、器官或组织,生物材料可结合至它们的表面。这些表面可大可小,且不一定要求均一,但是它们必须能够作为接触表面(不一定是单层的)。基底可以是有孔的、平坦的或非平坦的。基底包括接触表面,该表面可以是基底本身或者是有机或无机分子制得的第二层(例如,具有接触表面的基底或生物材料),表面用来与有机或无机分子接触。
本发明人曾经证明肽类能够与半导体材料结合。用于结合肽的半导体材料包括但不限于砷化镓、磷酸铟、硝酸镓、硫化锌、砷化铝、砷化镓铝、硫化镉、硒化镉、硒化锌、硫化铅、氮化硼和硅。
半导体纳米晶体表现出尺寸和形状依赖的光学和电学特性。这些多样的特性使得它们可用在多种装置上,例如发光二极管(LED)、单电子晶体管、光电的、光学和磁学存储器,以及诊断标记物和传感器。控制颗粒尺寸、形状和相位对于保护层是非常重要的,例如汽车涂层,和颜料如房屋的涂料。半导体材料可被加工成特定的形状和尺寸,其中这些半导体材料的光学和电学特性在多种装置中能得到最好的利用。
本发明人进一步开发了一种纳米颗粒成核的方法,以及介导它们自装配的方法。肽的主要特征在于它们能够识别并结合具有表面特异性的重要材料,以使尺寸受限的结晶半导体材料成核,并且控制成核纳米颗粒的结晶相。肽还可以控制材料的纵横比(aspect ratio),从而控制材料的光学特性。
简要地,生物系统能在非常微小的尺度上装配极其复杂结构的装置极大地激发了发明人想要找出具有类似作用的非生物系统。发明出用在令人感兴趣的电子或光学特性材料的方法将尤其具有意义,但是天然进化并未选择出在生物分子和这类材料之间相互作用。
本发明所基于的认识是,生物系统能够有效、精确地将纳米级的构成模块装配成具有高度完整性、受控的尺寸以及复合的均一性的具有复杂功能的结构。
一种提供随机有机聚合物池(random organic polymer pool)的方法是使用噬菌体展示文库。噬菌体展示文库是与M13大肠杆菌噬菌体的pIII包衣蛋白融合的7至12个氨基酸的随机肽形成的组合库,提供了能够与结晶半导体结构或其它材料相互作用的不同的肽类。在噬菌体颗粒一端具有pIII包衣蛋白的5个拷贝,它们在颗粒上为10-16nm。该噬菌体展示方法在多肽-基底相互作用和编码该相互作用的DNA之间提供了物理连接。
已经开发出了对各种材料,例如半导体和含元素碳的分子如碳纳米管和石墨,具有亲合力的肽序列。在下面的例子中使用了五种不同的单晶半导体,GaAs(100),GaAs(111)A,GaAs(111)B,InP(100)和Si(100)。这些半导体可以为肽相互作用提供系统评价,并且确认本发明方法在不同晶体结构上的一般实用性。此外,使用了含元素碳的分子,例如碳模板、高度有序的热解石墨(HOPG)和单壁纳米管(SWNT)导电胶。
使用噬菌体展示文库将与特定晶体成功结合的蛋白序列从晶体表面洗脱下来,扩增诸如百万倍,在更严格的条件下与基底反应。将这一过程重复3-7次,在库中选择具有最特异性结合肽的噬菌体。在经过例如第三、第四和第五次噬菌体筛选后,分离出晶体特异性的菌体,并对其DNA进行测序。鉴别对晶体组合物具有选择性的肽类结合(例如,与GaAs结合而不与Si结合)以及对晶面具有选择性的肽类结合(例如,与(100)GaAs结合,而不与(111)B GaAs结合)。
通过氨基酸功能分析方法,分析选自GaAs(100)的20个克隆,以确定针对GaAs晶面的表位结合域。图1所示为修饰的pIII或pVIII蛋白的部分肽序列,显示了与GaAs接触的肽中的类似结合域。随着与GaAs晶面接触的数量的增加,无电荷极性的和路易斯碱的官能团也增加。第三、四和第五个循环的噬菌体克隆序列分别平均包含30%、40%、和44%的极性官能团,而路易斯碱官能团的部分同时从41%增加至48%~55%。路易斯碱中观察到的增加仅占本发明文库的随机12-mer肽的官能团的34%,这说明肽上的路易斯碱和GaAs晶面的路易斯酸位点之间的相互反应可以介导由这些肽引起的选择性结合。
选自文库中修饰的12-mers的预期结构可以为伸展的构象,这应该对小肽类更合适,该构象使得肽比GaAs晶胞(5.65A°)更长。因此,在肽类对GaAs晶体的识别中,仅需要很小的结合域。这些短肽结构域,如图1所示,除了包含诸如天冬酰氨和谷氨酸盐等胺类路易斯碱(amine Lewis bases)外,还包含富含丝氨酸和苏氨酸的区域。为了确定精确的结合序列,已经用更短的文库对晶面进行筛选,该文库包括7-mer和二硫化限定的7-mer。使用这些更短的文库能减小结合域的大小和柔性,能够允许更少的肽-晶面相互作用,使得在所选的代之间的相互作用力产生预期的增加。
采用20-nm胶体金粒子标记的噬菌体用于定量检测特异性结合,其中的胶体金粒子用抗生物素蛋白链菌素(streptavidin)标记,并通过M13包衣蛋白的生物素化的(biotinylated)抗体与菌体结合。进行X-射线光电子分光光谱(XPS)化学成分分析,通过金4f-电子信号强度监测噬菌体与基底之间的相互作用(图2a-c)。在G1-3噬菌体不存在的情况下,XPS证实了抗体和金-抗生物素蛋白链菌素(gold-streptavidin)不与GaAs(100)基底结合。因此,该金-抗生物素蛋白链菌素的结合对噬菌体上表达的肽具有特异性,并且还是噬菌体与基底结合的指示剂。利用XPS还发现从GaAs(100)分离的G1-3序列与GaAs(100)而非Si(100)特异性结合(参考图2a)。在互补模式下,针对(100)Si晶面筛选的S1克隆几乎不与(100)GaAs晶面结合。
一些GaAs序列也与另一种闪锌矿结构--InP(100)的晶面结合。选择性结合的基础是化学的、结构的还是电子的结合仍处于研究之中。此外,基底表面的天然氧化物的存在能够改变肽结合的选择性。
已经证实了在GaAs的(111)A(镓末端,gallium terminated)或者(111)B(砷末端,arsenic terminated)的晶面上,G1-3克隆与GaAs(100)优先结合(图2b,c)。在(100)晶面的G1-3克隆的表面浓度要比在富含镓的(111)A或者富含砷的(111)B晶面的浓度高,其中(100)晶面用于选择。已知这些不同的晶面表现出不同的化学反应性,因此噬菌体与多种晶面的结合具有选择性也就不足为奇了。尽管两个111晶面的大末端(bulk termination)具有相同的几何结构,当对表面改造进行比较时,在表面双分子层具有Ga或As原子外层之间的差别是很明显的。还认为多种GaAs晶面的氧化组合物也是不同的,这反过来会影响肽结合的特性。
针对基底结合能的Ga 2p电子强度如2c所示,其中该基底与G1-3噬菌体克隆相接触。如图2b结果所预测,在GaAs(100),(111)A和(111)B的晶面观察到的Ga 2p强度与金浓度呈反比。在具有更高的金--抗生物素蛋白链菌素浓度的晶面上Ga 2p强度的降低是由于菌体在晶面覆盖的增加造成的。XPS是一种表面技术,其取样深度约为30埃;因此,由于有机层厚度的增加,使得来自无机基底的信号降低。利用该观测可以确定,金--抗生物素蛋白链菌素的强度实际上是由于GaAs晶面上存在包含晶体特异性结合序列的噬菌体。进行了与XPS数据相关的结合研究,其中将等量的特异性噬菌体克隆与具有相同晶面面积的不同半导体基底相接触。野生型的克隆(没有随机的肽插入)不与GaAs结合(未检测到菌斑)。对于G1-3克隆来说,从GaAs(100)表面洗脱的噬菌体群要比从GaAs(111)A表面洗脱下的数高12倍。
利用原子力显微镜(AFM)对结合到GaAs(100)和InP(100)上的G1-3,G12-3和G7-4进行成像。尽管In-P结合比GaAs结合具有更大的离子特性,但InP晶体具有与GaAs晶体同构的闪锌矿结构。通过AFM观测到的10-nm宽、900-nm长的噬菌体与通过透射电镜(TEM)观测到的M13噬菌体的尺寸相匹配,并观察到与M13抗体结合的金球与噬菌体结合(数据未显示)。InP晶面具有高浓度的噬菌体。这些数据表明许多因素影响基底的识别,包括原子尺寸、电荷、极性以及晶体结构等。
在TEM图像中观察到G1-3克隆(负染)与GaAs晶片结合(未显示)。数据证实了该结合通过G1-3的修饰的pIII蛋白来介导,而不是通过与主要的包衣蛋白的非特异性相互作用介导。因此,本发明的肽可在装配纳米结构和异质结构中用来介导特定的肽-半导体的相互作用(图4)。
用X-射线荧光显微镜来证明噬菌体与闪锌矿晶面的优选接触,其中闪锌矿晶面与不同的化学和结构组合物的表面密切接触。巢状的方块形(a nestedsquare pattern)被蚀刻成一GaAs晶片;该模块包含GaAs的1-μm线条,在每一线条之间有4μm的SiO2间隙(图3a,3b)。G12-3克隆与GaAs/SiO2形的基底相接触,洗涤以减少非特异性结合,用免疫荧光探针四甲基罗丹明(TMR)标记。发现标记的菌体为三条红线以及中央的圆点,相应于图3b中仅与GaAs结合的G12-3。该模块中SiO2区域未与噬菌体结合,为暗色区域。在未与菌体接触、但与一抗和TMR接触的对照组中没有观察到该结果(图3a)。利用未与菌体结合的G12-3肽得到相同的结果。
观察到GaAs克隆G12-3在AlGaAs上对GaAs具有基底特异性(图3c)。AlAs和GaAs在室温下具有基本相同的晶格属性(lattice constraints),分别为5.66A°和5.65A°,因此AlxGal-xAs的三重合金能够在GaAs基底上取向附生生长。GaAs和AlGaAs具有闪锌矿晶体结构,但是G12-3克隆仅对GaAs表现出结合选择性。采用包含GaAs和Al0.98Ga0.02As的交互层的多层基底。将基底材料进行裂解并随后与G12-3克隆相互反应。
G12-3克隆采用20-nm的金--抗生物素蛋白链菌素纳米颗粒进行标记。扫描电镜(SEM)的结果显示异质结构内GaAs和Al0.98Ga0.02As的交互层(图3c)。采用镓和铝的X-射线元素分析来绘制金--抗生物素蛋白链菌素颗粒的图谱,其中该颗粒仅针对异质结构的GaAs层,结果证实了对化学组合物的高水平结合特异性。在图3d中,显示了一种用于半导体异质结构的噬菌体鉴别的模型,如荧光和SEM图像中所见到的(图3a-c)。
本发明阐述了采用噬菌体展示文库来对有机肽序列和无机半导体基底之间的结合进行鉴别、开发和放大。对无机晶体的这种肽识别和特异性已经在GaAs、InP和Si上得到验证,并延伸至其它基底,包括使用本发明肽文库的GaN,ZnS,CdS,Fe3O4,Fe2O3,CdSe,ZnSe以及CaCO3。目前已经设计出具有两个成分识别的二价合成肽类(图4e);这类肽具有将纳米粒子定位在半导体结构特定位置上的能力。这些有机和无机对能够为下一代复杂的、综合性的电子结构加工提供有用的结构模块。
实施例1
肽的构建、分离、选择和定性
肽的选择。将噬菌体展示或肽文库与各种材料接触,例如在包含0.1%TWEEN-20的Tris-缓冲盐水(TBS)中的半导体晶体,以降低晶面上菌体-菌体之间的相互作用。在室温下摇动1小时后,用pH 7.5的Tris-缓冲盐水洗涤晶面10次,随着选择过程的进一步进行,该缓冲盐水中TWEEN-20的浓度从0.1%增加至0.5%(v/v)。噬菌体通过加入甘氨酸-HCl(pH 2.2)10分钟来破坏结合,因而从晶面上洗脱下来。将洗脱的噬菌体溶液转移至一新管中,然后用Tris-HCl(pH 9.1)中和。对洗脱下来的噬菌体进行浓度测定,比较结合能力。
将与基底接触三个循环后洗脱的噬菌体与其宿主Escherichia coli ER2537和ER2738混合,并置于LB XGal/IPTG平皿上。由于文库噬菌体来源于携带lacZα基因的M13mpl9载体,因此当噬菌体置于包含Xgal(5-溴-氯-3-吲哚基-β-D-半乳糖苷)和IPTG(异丙基-β-D-硫代半乳糖苷)的介质中时噬菌体菌斑显示为蓝色。采用蓝色/白色筛选法来选择具有随机肽插入的噬菌体菌斑。从平皿上收集菌斑并进行DNA测序。
基底制备。通过X-射线衍射对基底进行定位,采用适当的化学特异性蚀刻技术除去天然氧化物。在GaAs和InP晶面上检验下述蚀刻:在蚀刻时间的1分钟和10分钟时NH4OH∶H2O 1∶10,HCl∶H2O 1∶10,H3PO4∶H2O2∶H2O 3∶1∶50。采用HCl∶H2O 1∶10蚀刻1分钟,然后用去离子水漂洗1分钟可使GaAs和InP蚀刻晶面具有最佳的元素比例和最少的氧化物形成(使用XPS)。然而,由于在文库的初始筛选中对GaAs使用了氢氧化铵蚀刻,因此在所有其它GaAs基底实施例中都使用了该蚀刻。Si(100)晶片采用下述方法蚀刻:在HF∶H2O 1∶40中蚀刻一分钟,然后用去离子水漂洗。所有的晶面直接从漂洗液中取出后立刻转入噬菌体文库中。对照组基底的晶面不与噬菌体接触,通过AFM和XPS对晶面蚀刻过程的效果以及形态学进行定性及绘制图谱。
GaAs和Al0.98Ga0.02As的多重基底通过分子束取向附生(molecular beamepitaxy)在(100)GaAs表面上生长。取向附生生长层为5×1017cm-3水平的掺杂Si-的生长层(Si-doped)(n-型)。
抗体和金标记。在XPS,SEM和AFM的实施例中,基底在Tris缓冲盐水中与噬菌体接触1小时,然后转入fd噬菌体pIII蛋白的抗-fd噬菌体-生物素偶联物抗体(1∶500于磷酸盐缓冲液中,Sigma)中30分钟,然后用磷酸盐缓冲液漂洗。通过生物素-抗生物素蛋白链菌素相互作用,将抗生物素蛋白链菌素/20-nm胶体金标记(1∶200于磷酸盐缓冲盐水(PBS)中,Sigma)与生物素偶联的噬菌体联结;将晶面与标记接触30分钟,然后用PBS漂洗几次。
X-射线光电子光谱学(XPS)。制备下述对照用于XPS实例,从而确定在XPS所见的金信号是源于与噬菌体结合的金而不是与GaAs晶面的非特异性抗体的相互反应。将制备的(100)GaAs晶面与下述材料接触:(1)抗体和抗生物素蛋白链菌素-金标记,但没有菌体,(2)G1-3菌体和抗生物素蛋白链菌素-金标记,但没有抗体,以及(3)抗生物素蛋白链菌素--金标记,但没有G1-3菌体或抗体。
所用的XPS仪器为Physical Electronics Phi ESCA 5700,该仪器带有可产生单频1,487-eV X射线的铝阳极。噬菌体用金标记(如上文所述)后,立即将所有样品转入小室中来降低GaAs晶面的氧化,然后在高度真空下抽吸过夜,从而降低XPS小室中样品的除气作用。
原子力显微镜(AFM)。所用的AFM为安装了Zeiss Axiovert 100s-2tv的Digital Instruments Bioscope,采用针尖扫描模式(tapping mode)来运行。在空气中采用针尖扫描模式输出图像。AFM探针是蚀刻的硅,其带有125-mm支架,在其共振频率200±400kHZ附近驱动的弹性常数为20±100Nm-1。扫描速率为1±5mms-1。利用一级水平面使图像水平,从而去除样品的倾斜。
透射电镜(TEM)。利用Philips EM208在60kV获得TEM图像。G1-3噬菌体(在TBS中1∶100稀释)与GaAs片段(500mm)温育30分钟,离心使未结合的噬菌体与颗粒分离,用TBS漂洗,然后用TBS重悬。样品用2%乙酸双氧铀染色。
扫描电镜(SEM)。G12-3噬菌体(在TBS中1∶100稀释)与新鲜裂解的异质结构晶面温育30分钟,然后用TBS漂洗。G12-3噬菌体用20-nm胶体金标记。在5kV下利用Hitachi 4700型场发射式扫描电镜的Norian检测系统收集SEM和元素绘制图像。
实施例II.选择颗粒和取向特异性肽
已发现,半导体纳米晶体表现出尺寸和形状依赖的光学和电学特性,这些多样的特性使得它们可用在多种装置上,例如发光二极管(LED)、单电子晶体管、光电的、光学和磁学存储器,以及诊断标记物和传感器。控制颗粒尺寸、形状和相位对于保护层和颜料(汽车涂层,房屋的涂料)是非常重要的。为了利用这些光学和电学特性,有必要合成具有简洁尺寸和形状的结晶的半导体纳米晶体。
本发明包含组合物和用来选择以及使用多肽的下述方法:(1)识别并结合具有表面特异性的技术上重要的材料;(2)使尺寸受限的结晶半导体材料成核;(3)控制成核的纳米颗粒的结晶相;并(4)控制纳米晶体的纵横比以及,例如它们的光学特性。
该实施例中所用材料是族II-VI的半导体,包括下述材料:硫化锌、硫化镉、硒化镉和硒化锌。尺寸和晶体控制还可与钴、锰、氧化铁、硫化铁和硫化铅以及其它光学和磁学材料一起使用。使用本发明,熟练的技术人员能够创建无机-生物材料结构模块,用作复杂的电学装置和光电装置加工、以及环境和原位诊断新方法的基础,装置可以是例如发光显示器、光学检测器和激光、快速内部连线、波长选择开关、纳米级计算机元件和哺乳动物植入物。
图4-8表述了多肽的表达,使用例如噬菌体展示文库表达能与半导体材料结合的肽。分子生物学领域的技术人员会知道,可以使用其它表达系统在蛋白质表面以一种稳定的方式来表现短的或甚至长的肽序列。作为一个例子,可以在此使用噬菌体表现。噬菌体展示文库是一种含7-12个氨基酸的随机多肽组合物文库。多肽可与例如M13大肠杆菌噬菌体的pIII包衣蛋白融合,或形成嵌合体。噬菌体提供了能与晶体半导体结构反应的不同的多肽。由于在噬菌体颗粒一端具有pIII包衣蛋白的5个拷贝,它们在颗粒上为10-16nm,因此M13pIII包衣蛋白是非常有用的。该噬菌体展示方法在多肽-基底相互作用和编码该相互作用的DNA之间提供了物理连接。所测试的半导体材料包括ZnS,CaS,CaSe和ZnSe。
为了获得具有特异结合特性的多肽,将与特定晶体成功结合的蛋白序列从晶体表面洗脱下来,扩增诸如百万倍,在更严格的条件下与基底反应。将这一过程重复5次,在库中选择具有最特异性结合的噬菌体。在经过例如第三、第四和第五次噬菌体选择后,分离出晶体特异性的噬菌体,并对DNA测序来得到用于表面结合的多肽结构的密码。
在本发明的一个实施方式中,发现两个不同的肽使量子点的两个不同相成核。发现线性的12-mer肽Z8,它能生长硫化锌立方晶相的3-4nm的颗粒。分离出一种7-mer含二硫键的肽,A7,它能生长ZnS六角晶相的纳米颗粒。此外,这些肽影响纳米颗粒生长的纵横比。A7肽与噬菌体的p3连接或作为单层与金连接时,A7肽具有这种活性。此外,使A7融合到病毒表面的p8蛋白上,可以生长噬菌体/半导体纳米颗粒的纳米导线。在噬菌体表面生长的纳米颗粒表现出完美的ZnS颗粒晶体排列。
多肽控制纳米颗粒的尺寸,形态和纵横比:具有形状控制的氨基酸序列的噬菌体被分离并表征,选择出能与ZnS,CdS,ZnSe和CdSe晶体特异性结合的噬菌体。对这些多肽的结合亲和性和区别进行检测,根据检测结果,将多肽加工用于更高亲和性的结合。为了进行这些检测,根据mm尺度的多晶ZnS片筛选噬菌体文库。经过3、4和5轮筛选后,对结合克隆进行测序并放大。分析序列,并检测克隆的多肽使ZnS纳米颗粒成核的能力。
将命名为Z8、A7和Z10的克隆加到ZnS合成实验中,用于在室温的液态环境下控制ZnS颗粒尺寸和单分散性。ZnS特异性克隆与ZnCl2溶液中毫摩尔浓度的Zn+2离子反应。结合噬菌体的ZnS特异性肽作为加帽配体(capping ligand),当Na2S加到噬菌体-ZnCl2溶液中时形成了受控的晶体颗粒尺寸。
当加入毫摩尔浓度的Na2S,可观察到晶体材料呈悬浮状。使用透射电子显微镜方法(TEM)和电子衍射(ED)来分析悬浮液的颗粒尺寸和晶体结构。TEM和ED数据揭示了,与噬菌体克隆结合的ZnS特异性多肽的加入会影响所形成的ZnS晶体的颗粒尺寸。
观察到,在ZnS存在下生长的晶体为尺寸大约5nm的分散颗粒。而没有ZnS噬菌体克隆下生长的晶体则更大(>100nm),并且尺寸的范围也很大。
表1.ZnS特异性克隆的结合域(从氨基端至羧基端的写法)
A7 Asn Asn Pro Met His Gln Asn Cys(SEQ ID NO:232)
Z8 Val Ile Ser Asn His Ala Glu Ser Ser Arg Arg Leu(SEQ ID NO:72)
Z10 Ser Gly Pro Ala His Gly Met Phe Ala Arg Pro Leu(SEQ ID NO:233)
表2.CdS特异性克隆的结合域(从氨基端至羧基端的写法)
E1:Cys His Ala Ser Asn Arg Leu Ser Cys(SEQ ID NO:12)
E14:Gly Thr Phe Thr Pro Arg Pro Thr Pro Ile Tyr Pro(SEQ ID NO:14)
E15:Gln Met Ser Glu Asn Leu Thr Ser Gln Ile Glu Ser(SEQ ID NO:15)
JCW-96:Ser Pro Gly Asp Ser Leu Lys Lys Leu Ala Ala Ser(SEQ ID NO:28)
JCW-106:Ser Leu Thr Pro Leu Thr Thr Ser His Leu Arg Ser(SEQ ID NO:30)
JCW-137:Ser Leu Thr Pro Leu Thr Thr Ser His Leu Arg Ser(SEQ ID NO.:30)
JCW-182:Cys Thr Tyr Ser Arg Leu His Leu Cys(SEQ ID NO:234)
JCW-201:Cys Arg Pro Tyr Asn Ile His Gln Cys(SEQ ID NO:235)
JCW-205:Cys Pro Phe Lys Thr Ala Phe Pro Cys(SEQID NO:236)
在噬菌体产生的过程中表达了肽插入结构,例如使用具有二硫键的12-mer线性和7-mer的限制性文库也能得到类似的结果。
使用12个氨基酸线性文库和7个氨基酸限制性环形文库相比,所选的针对ZnS的多肽对于ZnS的晶体结构和ZnS纳米晶体的纵横比有重要的影响。
展示出针对ZnS的12mer线性多肽的噬菌体的存在下,生长的纳米颗粒的高分辨晶格图像显示出ZnS立方形状(锌-闪锌矿)的晶体生长了3-4nm范围(1∶1纵横比)。相比之下,所选的用于结合ZnS的7mer限制性多肽生长出ZnS六角形(wurzite)的椭圆形的颗粒和线(2∶1纵横比和8∶1纵横比)。因此,可以通过调节肽的长度和序列来改变纳米晶体的特性。进一步,晶体的电子衍射图说明来自不同克隆的多肽能使ZnS的两种不同晶体结构得到稳定。Z8的12mer肽能稳定锌-闪锌矿结构,A7的7mer限制性肽能稳定wurzite结构。
图10揭示了经过3、4和5轮选择后的ZnS多肽的序列进化。用7mer限制性文库进行的肽选择,经过第5轮选择后获得了最佳结合的肽序列。该序列命名为A7。第5轮选择后,大约30%的分离克隆具有A7序列。在第3轮的选择后,发现第7位上的ASN/GLN非常重要。在第四轮选择中,ASN/GLN在第1和2位上也显得非常重要。这种重要性在第5轮中进一步增强。在第3、4和5轮中,序列第2位上的阳性电荷非常明显。图11是根据本发明的第5轮选择后氨基酸的取代情况。
在A7序列上进行位点突变来测试结合亲合力的变化。突变包括:第3位:his ala;第4位:met ala;第2位:gln ala;以及第6位:asn ala。这些突变可以在肽序列上共同进行,单个进行或组合进行。
与ZnS结合的氨基酸序列的结构域为(氨基端至羧基端的写法):酰胺-酰胺-Xaa-Xaa-positive-酰胺-酰胺或ASN/GLN-ASN/GLN-PRO-MET-HIS-ASN/GLN-ASN/GLN(SEQ IDNO:237)。
与外源的克隆和基底相比,通过结合研究分离的针对ZnS的克隆表现出对该ZnS基底具有优先的相互作用。
不同克隆与不同基底例如FeS、Si、CdS和ZnS之间的相互作用说明:通过与ZnS的结合研究分离到的克隆表现出与ZnS具有优先的相互作用。简单地说,洗涤和感染后,对噬菌体滴度进行计数和比较。对Z8和Z10而言,除了ZnS以外的任何基底都没有明显的滴度计数。没有多肽插入片段的野生型克隆被用作对照,来确认插入的片段的确介导了所要的相互作用。没有多肽就不会产生特异性结合,滴度计数为零。
将用在几种不同ZnS克隆上的相同的结合方法进行比较。具有不同肽插入片段的克隆在相同浓度下与ZnS的类似大小片段作用1小时。重复清洗基底-噬菌体复合物,通过改变pH将结合的噬菌体洗脱下来。洗脱物用来感染细菌,过夜培养后进行空斑计数。Z8表现出对所选的12mer线性肽的ZnS最强的亲合力。野生型没有表现出对ZnS晶体的结合能力。Z8、Z10和野生型肽不与Si、FeS或CdS晶体结合。
纳米晶体在肽功能化表面的合成和装配得到了确定。已单独测试A7肽控制ZnS结构的能力。当与噬菌体结合时,A7肽能特异性选择并生长ZnS晶体;将A7肽用于金基底的功能化表面的形成,该基底能介导从溶液中形成ZnS纳米晶体。将制备自装配单层的方法用在制备功能化表面上。
为了确定A7在形成ZnS纳米晶体上的能力和选择性,使金基质上具有不同表面化学性质的不同类型的表面与ZnS前体溶液接触。ZnCl2和Na2S可用作ZnS前体溶液。CdCl2和Na2S的CdS前体溶液用来提供CdS。在四个表面形成的晶体可通过SEM/EDS和TEM来表征。
对照表面1由空白的金基底组成。在ZnS溶液或CdS溶液中老化(aged)70小时后,就观察不到晶体的形成了。对照表面2由金基底上的2-巯基乙胺自装配单层组成。该表面不能诱导ZnS和CdS纳米晶体的形成。在某些位置上能观察到ZnS沉淀。对于CdS体系,能观察到零星分散的2微米CdS晶体。当Cd+2和S-2的浓度在1×10-3M时,会产生这些晶体的沉淀。
第三次表面测试是在仅有A7功能化的金表面进行的。该表面能介导5nm的ZnS纳米晶体的形成,但是不能介导CdS纳米晶体的形成。
第四次表面测试是在A7-酰胺功能化的金表面上进行的,该表面通过在A7肽溶液中使对照表面2老化(aging)而制得的。在表面上形成的ZnS晶体为5nm,CdS晶体为1-3um。CdS晶体还可在只有胺的表面上形成。
从四个表面的结果来看,A7肽能介导ZnS纳米晶体的形成,但是不能介导CdS纳米晶体的形成。此外,所选的针对CdS的肽能使CdS纳米颗粒成核。
能使半导体材料特异性成核的多肽被表达至M13的p8主要包衣蛋白上。已知p8蛋白能自组装成一个高度定向的晶体蛋白外壳。目前的假说认为,如果多肽插入物能以高拷贝数表达,那么纳米p8蛋白的晶体结构就能转到多肽插入物中。并且还可预见到,如果所要的多肽插入物保持一种相对于p8外壳的晶体取向,那么从这个肽插入物成核的晶体就会生长与晶体形状相关的纳米晶体。这种预见已通过高分辨率的TEM得到测试并确认。
图12是用于形成纳米导线的p8和p3插入物的示意图。成核的ZnS纳米颗粒与融合至M13噬菌体p8蛋白外壳的A7肽脱离,而制备得到了Zns纳米导线。ZnS纳米颗粒包被噬菌体的表面。ZnS在M13噬菌体外壳成核的HRTEM影像表明,在噬菌体外壳成核的纳米晶体由非常好的取向性,其中M13噬菌体外壳在p8蛋白上有A7肽插入。目前还不清楚噬菌体外壳是否是p8-A7融合包衣蛋白和野生型的p8蛋白的混合物。在Z8肽插入物上也进行了类似的实验,尽管ZnS晶体也在噬菌体上成核,但是它们相互间并没有取向性。
原子力显微镜(AFM)用来使结果成像,表明p8-A7自装配晶体包被噬菌体的表面,从而在A7肽序列位置的嵌合蛋白顶部产生了纳米导线(数据未显示)。在M13外壳的p8-A7融合位置处使ZnS纳米颗粒成核而制备得到纳米导线。
在p8蛋白具有A7肽插入物的M13噬菌体外壳上的ZnS纳米晶体成核得到了高分辨TEM的确认。尽管发现在p8-A7融合包被蛋白中混合入了一些野生型p8蛋白,还是获得了晶体成核。如晶格成像所揭示(数据未显示),在噬菌体外壳上成核的纳米晶体有极好的取向性。数据表明,多肽能够以极佳的取向保守性表现在主要包衣蛋白上,并且这些有取向的肽能够使取向单分散的ZnS半导体纳米颗粒成核。
这些积累的数据表明,某些多肽能够以极佳的取向保守性表现在主要包衣蛋白上,并且这些肽能够使有取向的ZnS半导体纳米颗粒成核。
肽的选择。将噬菌体展示或肽文库与半导体或其它晶体在包含0.1%TWEEN-20的Tris-缓冲盐水(TBS)中相接触,以降低表面上菌体-菌体之间的相互作用。在室温下摇动1小时后,用pH 7.5的Tris-缓冲盐水接触10次来洗涤晶面,随着选择次数的进行,将该缓冲盐水中TWEEN-20的浓度从0.1%增加至0.5%(v/v)。通过加入甘氨酸-HCl(pH 2.2)10分钟来破坏结合力,使噬菌体从表面上洗脱下来。洗脱下来的噬菌体溶液转移至一新管中,然后用Tris-HCl(pH 9.1)中和。对洗脱下来的噬菌体进行浓度测定,比较结合能力。
将与基底接触三个循环后洗脱的噬菌体与宿主Escherichia coli ER2537或ER2738混合,并置于Luria-Bertani(LB)XGal/IPTG平皿上。由于文库噬菌体来源于携带lacZα基因的M13mp19载体,因此当噬菌体置于包含Xgal(5-溴-氯-3-吲哚基-β-D-半乳糖苷)和IPTG(异丙基-β-D-硫代半乳糖苷)的介质中时噬菌体菌斑或感染区域显示为蓝色。采用蓝色/白色筛选法来选择具有随机肽插入的噬菌体菌斑。从平皿上收集菌斑分离DNA并进行测序。
原子力显微镜(AFM)。所用的AFM为安装了Zeiss Axiovert 100s-2tv的Digital Instruments Bioscope,采用针尖扫描模式(tapping mode)来运行。在空气中采用针尖扫描模式输出图像。AFM探针是蚀刻的硅,其带有125-mm支架,在其共振频率200±400kHZ附近驱动的弹性常数为20±100Nm-1。扫描速率为1±5mms-1。利用一级水平面使图像水平,从而去除样品的倾斜。
透射电镜(TEM)。用JEOL 2010和JEOL 200CX透射电镜获得TEM图像。所用的TEM栅是在金上的碳。没有进行染色。样品生长后,根据分子量对反应混合物进行浓缩,截去滤过物,用无菌水清洗4次去除过多的离子或未结合噬菌体的颗粒。浓缩至20-50ul后,将样品在TEM或AFM样品栅中干燥。
实施例III.对含碳元素分子有亲合力的生物材料
在该实施例中,采用噬菌体展示技术来测定对碳模板、高度有序的热解石墨(HOPG)以及单壁纳米管(SWNT)导电胶有亲合力的7-和12-mer肽序列。从淘洗(Biopanning)中筛选到的噬菌体克隆中,克隆Graph5-01(N′-WWSWHPW-C′)(SEQ ID NO:238)和Graph53-01(N′-HWSWWHP-C′)(SEQ ID NO:239)能在噬菌体结合研究中以最高的效率与碳模板结合。克隆Hipcol2R44-01(N′-DMPRTTMSPPPR-C′)(SEQ ID NO:196)与SWNT导电胶结合效果最好。
用荧光素标记抗-M13噬菌体的抗体来标记噬菌体,并使用共聚焦显微镜使它们在基底上成像,以便确定这些菌体与对应的基底结合的能力。共聚焦显微镜还可用来使基底与荧光标记的合成肽间的结合成像,其中合成肽包含基底特异性序列。AFM测定表明,克隆Graph5-01表现出对HOPG的交叉反应性。其它方法的例子如下所述。
淘洗:碳模板(来自Ted Pella,Inc.,尺寸为大约12.7mm直径×1.6mm厚度;每片大约5×2×1.6mm)以及高度有序的热解石墨(HOPG)(来自University of Texas at Austin)被用作掏洗的石磨源。SWNT导电胶被塑造成雪茄状的聚集体(至少0.1g净重),淘洗前,干燥至少一个晚上(最后的干重为约0.05g)。PhD-C7C和PhD-12mer文库来自New England Biolabs,Inc.(Beverly,MA),根据厂商说明书来进行淘洗。每种基底的淘洗重复至少一次。
噬菌体克隆命名:根据碳模板选出的噬菌体克隆的名称前加“Graph”。根据SWNT导电胶选出的噬菌体克隆前加“hipco”。根据HOPG选出的噬菌体克隆前加“HOPG”。具有12-mer插入物的所选的克隆命名为:(基底)12R(round#)(round repeat#)-(SEQ ID NO:);而具有限制性的7-mer插入物的克隆被命名为:(基底)(round#)(round repeat#)-(SEQ ID NO:)。
肽:生物素化的肽Hipco2B(N′-DMPRTTMSPPPRGGGK-C′-生物素)(SEQ ID NO:244)由Genemed Synthesis,Inc.(San Francisco,CA)合成。生物素化的肽GraphitelB(N′-ACWWSWHPWCGGGK-C′-biotin)(SEQ ID NO:240),JH127B(N′-ACDSPHRHSCGGGK-C′-生物素)(SEQ ID NO:241),和JH127MixB(N′-ACPRSSHDHCGGGK-C′-生物素)(SEQ ID NO:242)是由ICMB Protein Microanalysis Facility(University of Texas at Austin)合成,并通过反向HPLC(HiPore RP318250×10mm column,BioRad,Hercules,CA,acetonitrile gradient)来纯化。根据化学领域公知的碘氧化方法,在Graphite1B肽的半胱氨酸之间形成二硫键,得到环化的Graphite1B肽。使用电子发射离子质谱(EsquirLC00113,Bruker Daltonics,Inc.,Billerica,MA)来确认肽的纯度和分子量。
噬菌体结合研究:干燥、平滑和方形的SWNT导电胶(至少约0.05g湿重,0.0025g干重),以及至少约0.04g的碳模板用于结合研究。使用前,至少进行两次噬菌体克隆的扩增和测定滴度(根据噬菌体文库的厂商说明书)。每种噬菌体克隆的相同量(至少约5×1010pfu)分别与SWNT/碳模板(例如,聚集体)在1ml的TBS-T[50mM Tris,150mM NaCl,pH 7.5,0.1%Tween-20]室温下温育1小时,并在离心管中摇动。然后用TBS-T清洗聚集的表面9-10次(每次1ml),通过与0.5ml的0.2M甘氨酸HCl(pH 2.2)接触8分钟来从表面上洗脱噬菌体。洗脱的噬菌体立即被转移到新管中,用0.15ml的1M Tris HCl(pH 9.1)中和,然后分两份测滴度。每个结合实验都进行两次。在本发明的一个实施方式中,使用SWNT聚集体并用相同聚集体(用于初始实验)的重复结合研究包括:首先用1ml 100%的乙醇洗1小时,然后用1ml的水洗两次。
共聚焦显微镜:使用前,至少进行两次噬菌体克隆的扩增和测定滴度(根据噬菌体文库的厂商说明书)。每种噬菌体克隆的相同量(5×109pfu)分别与碳模板片或少量的湿SWNT导电胶在0.2-0.3ml的TBS-T在微量离心管中室温下温育1小时,并偶尔摇动。碳模板/SWNT聚集物然后用TBS-T清洗两次(每次1ml),与0.2-0.3ml的生物素化的鼠单克隆抗-M13抗体(在TBS-T中稀释1∶100,Exalpha Biologicals,Inc.,Boston,MA)温育45分钟。聚集物然后用TBS-T洗两次(每次1ml),与0.2-0.3ml的抗生物素蛋白链菌素-荧光素(在TBS-T中稀释1∶100,Amersham Pharmacia Biotech,Uppsala,Sweden)温育10分钟,然后用TBS-T清洗两次(每次1ml)。然后将过量的液体从聚集物中去除。SWNT导电胶重悬于Gel/Mount(Biomedia Corp.,Foster City,CA)中,并置于载玻片上用No.1盖玻片覆盖。碳模板置于涂有真空油脂的载玻片上,用Gel/Mount覆盖,上面再放置盖玻片。对于SWNT导电胶样品,每一次标记和清洗步骤还需要离心。
在微量离心管中,肽(至少为1mg/ml)分别与碳模板片或少量的湿SWNT导电胶在0.15ml的TBS-T中温育1小时,并偶尔摇动。发现初始的Hipco2B的10mg/ml储液能溶于55%的乙腈和含环化的和非环化的Graphite1B的45%乙腈中。用TBS-T稀释时,这些肽形成了白色的沉淀。基底然后用TBS-T洗2-3次(每次1ml),与0.15ml的抗生物素蛋白链菌素-荧光素(在TBS中稀释1∶100)温育15分钟,再用TBS洗2-3次(每次1ml)。去除基底上过量的液体。SWNT导电胶重悬于Gel/Mount中,并置于载玻片上用No.1盖玻片覆盖。碳模板置于涂有真空油脂的载玻片上,用Gel/Mount覆盖,上面再放置盖玻片。对于SWNT导电胶样品,每一次标记和清洗步骤还需要离心。
用Leica TCS 4D共聚焦显微镜(ICMB Core Facility,University of Texasat Austin)获得共聚焦成像。图象代表最大强度的合成物。
AFM:使用前,至少进行两次噬菌体克隆的扩增和测定滴度(根据噬菌体文库的厂商说明书)。每种噬菌体克隆的相同量(5×109pfu)分别与刚切割的HOPG层在2ml TBS中温育1小时,置于35mm×10mm的培养皿中摇床培养。然后将基底转移至微量离心管中,用水清洗两次(每次1ml),过夜干燥。用Multimode Atomic Force Microscope(Digital Instruments,Santa Barbara,CA)采用针尖扫描模式(tapping mode)获取图像。
淘洗序列:含有12-mer和限制性的7-mer序列插入到pIII包衣蛋白上的M13噬菌体文库被用来筛选对碳模板、HOPG和SWNT导电胶具有特异性的克隆。
碳模板:利用针对碳模板的phD-C7C文库的第四轮筛选产生了一个优势噬菌体克隆,该克隆具有肽插入序列N’-WWSWHPW-C’(SEQ ID NO:238),参见图13。重复这一筛选过程,则在第四轮得到了类似的优势序列N’-HWSWWHP-C’(SEQ ID NO:239)和一个稍弱的优势序列N’-YFSWWHP-C’(SEQ ID NO:243)。PhD-12文库筛选在第五轮产生了相同的序列N’-NHRIWESFWPSA-C’(SEQ ID NO:172),重复筛选会在第六轮产生序列N’-VSRHQSWHPHDL-C’(SEQ ID NO:179)和N’-YWPSKHWWWLAP-C’(SEQ ID NO:180),如图14所示。这些序列富含芳香残基,且一般包括残基S,W,H和P。在本发明的一个实施方式中,在phD-12文库筛选的第五轮中观察到了N’-SHPWNAQRELSV-C’(SEQ ID NO:178),但它是针对SWNT导电胶淘洗的污染序列,在后续筛选中消失了。
SWNT导电胶:由于所选的噬菌体中野生型噬菌体克隆(pIII不含有肽插入物)占优势,导致针对SWNT导电胶的PhD-C7C淘洗的失败。如图15所示,在PhD-12文库的第四轮选择中,获得了相同的序列N’-SHPWNAQRELSV-C’(SEQ ID NO:178),选择过程的第二和第三次重复产生了序列N’-LLADTTHHRPWT-C’(SEQ ID NO:192),N’-DMPRTTMSPPPR-C’(SEQID NO:196)和N’-TKNMLSLPVGPG-C’(SEQ ID NO:195)。
HOPG:没有进行利用phD-C7C文库对HOPG筛选的实验,但是在phD-12文库第五轮筛选中产生了优势序列N’-TSNPHTRHYYPI-C’(SEQ IDNO:219),和稍弱的优势序列N’-KMDRHDPSPALL-C’(SEQ ID NO:221)和N’-SNFTTQM TFYTG-C’(SEQ ID NO:220),如图16所示。(注意:在第一轮筛选中也观察到了N’-LLADTTHHRPWT-C’(SEQ ID NO:192),但发现它是针对SWNT导电胶淘洗的污染序列。)
从淘洗中获得的许多主要序列的实施例见表3。
表3:从掏洗中获得的相同序列(N’-到C’-末端)的实施例
噬菌体结合研究:根据淘洗确定的不同噬菌体克隆的相对结合效率通过下述步骤测定:碳模板和SWNT导电胶聚集体分别与每种噬菌体克隆的相同量(5×1010pfu)接触1小时,用TBS-T清洗,然后测定每种剩余的克隆与基底表面结合的滴度。用0.2M甘氨酸HCl,pH2.2将结合的噬菌体从基底上洗脱下来,测滴度来定量分析。用于这些实验的克隆如表4所示。A7(限制性7-mer插入物)和Z8(12-mer插入物)克隆和野生型克隆用作阴性对照。
表4:用于噬菌体结合研究的噬菌体克隆的PIII插入物
噬菌体克隆 | 文库来源 | PIII插入物(N’-至C’-末端) |
Hipco12R4-01 | PhD-12 | SHPWNAQRELSV(SEQ ID NO:178) |
Hipco12R42-01 | PhD-12 | LLADTTHHRPWT(SEQ ID NO:192) |
Hipco12R44-01 | PhD-12 | DMPPTTMSPPPR(SEQ ID NO:196) |
Hipco12R44-03 | PhD-12 | TKNMLSLPVGPG(SEQ ID NO:195) |
Graph5-01 | PhD-C7C | WWSWHPW(SEQ ID NO:238) |
Graph53-01 | PhD-C7C | HWSWWHP(SEQ ID NO:239) |
Graph53-05 | PhD-C7C | YFSWWHP(SEQ ID NO:243) |
Graph12R5-01 | PhD-12 | NHPIWESFWPSA(SEQ ID NO:245) |
Graph12R62-01 | PhD-12 | VSRHQSWHPHDL(SEQ ID NO:179) |
Graph12R62-02 | PhD-12 | YWPSKHWWWLAP(SEQ ID NO:180) |
A7 | PhD-C7C | NNPHMQN(SEQ ID NO:229) |
Z8 | PhD-12 | VISNHAESSRRL(SEQ ID NO:230) |
Graph4-18 | PhD-12,-C7C | 无插入(野生型) |
如图17所示(A和B),噬菌体克隆Hipco12R44-01与SWNT导电胶结合的数量高于所有其它的SWNT-或碳模板特异性克隆,如图18所示的克隆Graph5-01和Graph53-01能高效地与碳模板结合。针对碳模板选出的克隆只观察到与SWNT导电胶极弱的交叉反应性。此外,针对SWNT导电胶选出的克隆不与碳模板发生交叉反应性。
从淘洗过程中获得了几个相同的序列,但不是淘洗选出的所有噬菌体克隆都是有效的结合物(即,“有效”意思是经该类型的结合或亲合研究,对基底的亲合力比野生型克隆强)。在这些结合研究中,使用洗脱缓冲液不能完全从基底上全部去除结合的噬菌体,这可能是解释这些实验时的一个错误来源。这些结果还可能说明了针对每个基底选择和测试几种相同序列的重要性(即,重复的淘洗可产生更好的序列)。
通过共聚焦显微镜在基底上使噬菌体和肽成像
碳模板:如图19所示,碳模板特异性的噬菌体克隆(Graph5-01和Graph53-01噬菌体)与基底结合的成像采用下述步骤:使碳模板片分别与等量(5×109pfu)的每种克隆接触1小时,用生物素化的抗-M13抗体标记噬菌体,用抗生物素蛋白链菌素-荧光素标记抗体,通过共聚焦显微镜使复合物显示图像。(所有图像均为250μm×250μm,除非另有标注。)噬菌体克隆Hipco12R44-01,JH127(97μm×97μm)(来自Sandra Whaley,具有限制性pIII插入物N′-DSPHRHS-C′)(SEQ ID NO:231))以及野生型(Graph4-18,没有插入物)克隆用作阴性对照。与上述的噬菌体结合研究结果一致,碳模板与克隆Graph5-01的结合效率最高,其次是与Graph53-01的结合效率,如图19所示。在基底和克隆JH127间观察到了相当强的交叉反应性,但是在克隆Hipco12R44-01或野生型克隆与碳模板之间观察到的结合非常弱。
碳模板与对应于上述噬菌体pIII插入物的肽序列之间的结合也可通过共聚焦显微镜成像。等量(1mg/ml)的环状肽Graphite1B(对应于克隆Graph5-01)、非环状肽Graphite1B、肽Hipco2B(对应于克隆Hipco12R44-01)、肽JH127B(对应于克隆JH127)以及肽Jh127MixB(对应于克隆JH127但是具有混合的氨基酸序列)分别与碳模板接触1小时,然后用抗生物素蛋白链菌素-荧光素标记。
如图20所示,在未进行肽温育的样品中,观察到了检测量的背景荧光,表明在抗生物素蛋白链菌素-荧光素与基底之间发生了非特异性结合。这个结果很可能是由于该特定实验中清洗不充分造成的,因为在图19所示的实验中,一个即没有接触噬菌体也没有接触肽的类似样品没有显示背景荧光。尽管有背景荧光,与非环状Graphite1B接触的样品比其它样品显示出更强的荧光。相比之下,环状Graphite1B和Hipco2B样品显示的荧光没有比背景强,表明Graphite1B的环化干扰了基底的结合(图像250μm×250μm)。在基底与肽JH 127B和J H 127MixB之间观察到的结合稍微强一些。Graphite1B、JH127B和JH127MixB肽共有的氨基酸残基是S、P和H。在后续的肽与碳模板结合成像的共聚焦实验中应使用更高浓度的肽来提高荧光强度,并更注意清洗步骤以减少背景。
SWNT导电胶:图21显示了SWNT导电胶与噬菌体克隆以高亲合力与SWNT导电胶(Hipco12R44-01)结合的共聚焦成像(图像250μm×250μm)。Graph5-01以及野生型(Graph4-18,没有插入物)克隆用作阴性对照。Hipco12R44-01克隆显示出了高程度的荧光现象,而在对照样品上也观察到了一定程度的荧光。在没有噬菌体的情况下,没有背景荧光,这表明在Graph5-01以及野生型样品上的荧光不是由于非特异性基底与抗体或抗生物素蛋白链菌素-荧光素的结合。尽管在这些共聚焦结合研究中所用的噬菌体浓度(5×109pfu在0.2-0.3ml=1.7-2.5×1010pfu/ml)与在噬菌体结合中所用的浓度是相同数量级的(5×1010pfu in 1ml=5×1010pfu/ml),但在图17所示的噬菌体结合研究中只观察到非常少量的Graph5-01或野生型克隆与SWNT导电胶结合。在这两个实验中观察到的结合差异可能是由于SWNT导电胶基底制备和处理的方式造成的。在共聚焦实验中用到的湿的、具有延展性的SWNT导电胶的离心方法会导致在基底上同时捕获特异性和非特异性的噬菌体,而在噬菌体结合研究中使用大的干燥过的SWNT聚集体则不会有这一结果。在共聚焦实验中使用了湿的导电胶以便能放置在盖玻片下,但是以后的共聚焦结合实验应使用干燥的SWNT聚集体。
同样还制备了一种经上述用到的噬菌体克隆的pIII插入物对应的肽序列处理过的SWNT导电胶,但是没有成像。
使用AFM在HOPG上的噬菌体成像
由于基底表面的粗糙,因此不能采用AFM分析碳模板和SWNT导电胶上的噬菌体结合。然而,可以使用HOPG,结果参见图22。观察到噬菌体克隆Graph5-01(碳模板特异的)与HOPG结合,但是在HOPG上没有观察到野生型克隆。
噬菌体的结合研究以及本实施例中采用共聚焦显微镜观察到的肽和噬菌体与碳模板的结合一致说明:序列N’-WWSWHPW-C’(SEQ ID NO:238)和N’-HWSWWHP-C’(SEQ ID NO:239)能最高效地与碳模板结合。噬菌体结合实验还揭示了噬菌体克隆Hipco12R44-01(N’-DMPPTTMSPPPR-C’)(SEQ ID NO:196)与SWNT导电胶的结合效率最高。
在噬菌体结合研究和碳模板特异性噬菌体克隆与SWNT导电胶之间的共聚焦实验中几乎观察不到交叉反应性。尽管存在于碳模板和SWNTs上的石墨结构在理论上非常类似。也有可能在本研究所用的原料导电胶中的SWNTs壁含有污染物和/或被氧化作用破坏。为了减少由于存在可能的污染物而导致的有限的交叉反应(即,高特异性),希望可以采用更纯的纳米管原料。
实施例IV:使用与含碳元素分子有亲合力的生物材料
下面的实施例是阐述本发明的应用,其中用到了SEQ ID NOS:1-245。此外,还可使用本发明的方法和组合物与其它含碳分子。
分离金属的和半导电的CNT
目前制备单壁碳纳米管(SWNT)的合成方法会产生金属的和半导电的SWNTs混合物。为了加工纳米级的电子设备,分离金属的SWNT和半导电的SWNTs是及其有利的。金属的和半导电的SWNTs之间微小的形状和对称差异可通过快速-进化的蛋白质来区分,该蛋白质是利用噬菌体展示文库或类似的方法来获得的。根据噬菌体展示结果选出的蛋白质序列,可能会构建反向柱来纯化金属的和半导电SWNTs的混合物。如果金属的和半导电SWNTs的混合物通过反向柱,则肽与一种金属的或半导电SWNTs之间的特定的相互作用会导致洗脱时间的差异。如果金属SWNTs结合肽用于反向柱,则半导电SWNTs的洗脱比金属SWNTs快。因此,可分离到一种特异性SWNT。图23是SWNTs纯化反向柱的示意图。
碳纳米管的排列
碳纳米管用作纳米级装置的一个最大挑战是在三维阵列上排列纳米管。尽管化学气相沉积(CVD)方法可从加工中产生独特的排列结构,CVD方法还可产生金属的和半导电的SWNTs的混合物。由于纳米-电子装置的加工是很精确的,因此从混合物中分离半导电的SWNTs非常有益。可根据前述的方法进行分离。尽管在本实施例中使用了几种方法,例如LB-膜方法和半月板力控制(meniscus force control)等,这些方法仅提供了定向SWNT排列。当使用了对SWNTs具有特定结合性质的噬菌体时,构建了位置和定向排列的SWNT的二维或三维结构。如图24所示的由噬菌体连接的SWNTs就像二段共聚物,由肽单元将两个刚性的模块连接起来。可以预见,SWNT连接的噬菌体结合模块能产生微观分离的薄层状结构,得到结构是排列的SWNT结构。
通过肽连接P-N与SWNT
在没有任何化学修饰的情况下,半导电SWNTs一般具有内在p-型电学特性。进行电子提供基团的化学修饰会使p-型SWNT转换成n-型SWNT。通常具有分离的正电荷和负电荷蛋白域的周期性结合肽会导致SWNTs的电学特性。具有周期性负电荷和正电荷域的SWNTs具有P-N联合半导体结构的相同结构。这些P-N联合的相互连接可能会导致FET和复杂整合的电路功能的更高结构,例如与非门、或非门、与门和或门。使用SWNT结合肽的n-型SWNT修饰的示意图见图25。这些相同的修饰可用在多壁纳米管和多壁纳米管导电胶上。
纳米管的溶解性和生物相容性
在溶剂中的低溶解度会阻碍SWNT的进一步应用。一般来说,在水中的溶解对SWNT的生物学应用是很重要的。尽管在本实施例中使用包装聚合物和表面活性剂来溶解SWNT,但是它们必须进一步应用于生物系统中。可以相信,偶联了识别SWNT表面的肽的亲水性肽基团可使SWNT溶解在水中。此外,亲水性肽基团的去除可用来帮助SWNTs溶解在非极性溶剂中。这些同样的修饰可用在多壁纳米管和多壁纳米管导电胶上。
半导电SWNT的布线(wiring)
根据本发明,识别SWNT(金属的和半导电的)的肽会被布在一起来形成整合的SWNT电路,并且作为功能电子设备。类似的,布线技术可用在多壁纳米管和其它含碳元素分子中。
生物传感器
生物相容性SWNTs可用作生物传感器来检测微生物上的微小化学和物理变化。金属SWNTs的传导性一般会受到SWNTs周围电子分配的强烈影响。这样,通过检测SWNTs的传导性可监控生物相互作用,其中SWNTs偶联两个识别结构域:一个是针对SWNT的,另一个是针对生物靶物质的。当生物靶检测--肽与靶分子结合时,SWNTs的电子分布可受周围肽的影响。肽的结合与非结合状态可受到电子信号的监控,并直接用作生物传感器,例如抗原-抗体检测,血糖检测,及其它。使用本发明的方法和组合物,多壁纳米管或其它含碳元素的分子也可用作生物传感器。
此外,与SWNT结合的肽链的构象还受到pH、离子强度、金属离子浓度和温度变化的影响。这些环境变化还可影响SWNTs的电子分布。所有这些变化都可使用SWNTs结合肽来检测。
8.药物释放系统
SWNTs可用作坚固的支架来包含药物。此外,SWNTs还可用来传递药物,尤其是当SWNTs结合肽被药物修饰时。例如,由肽连接的药物可随时间缓慢释放。一般来说,这些药物以类似于膜片型(patch-type)药物传递系统来发挥功能。SWNT用作药物释放系统的示意图如图26。此外,药物可直接植入到病灶处,例如肿瘤细胞。
其它含碳元素的分子还可用作本发明的释放药物的药物组合物、诊断标记物、和/或药物,本发明的方法及组合物可用于预防治疗、治疗、诊断、监控和/或筛选(例如,药物、症状、相互作用,和/或效果)。
癌症治疗
生物相容的CNT可用作放射性的或高毒性药物传递介质。此外,利用与MWNT有特定结合性质的肽,多壁碳纳米管(MWNT)可转换成生物相容的MWNT。MWNTs通常含有至少3-4nm的MWNT管道。该MWNT管道可被高毒性或放射性药物填充,作为化学/放射治疗的特定用途。包含高毒性或放射性药物的MWNTs可直接植入肿瘤细胞或器官,然后根据预定的要求释放高毒性或放射性药物。通过改变内管道的直径可控制释放速度。在肿瘤药物治疗中应用SWNTs的示意图请参见图27。
其它含碳元素的分子还可用于药剂的治疗性传递,作为治疗工具或对疾病发展(例如,对于肿瘤或其它病理状况)的监控。
本发明可含有或不含有上述的全部组分。例如,在没有基底的情况下可制得本发明的生物支架。此外,本发明的方法和组合物可用在光学、微电子、磁学和工程领域。这些应用包括合成含碳材料、碳纳米管排列、创建生物半导体、单壁纳米管导电胶的连接转换、多壁纳米管导电胶的连接转换、促进单-和多-壁纳米管导电胶的溶解性和生物相容性、制备整合的单-和多-壁纳米管导电胶、生物传感器的制备、药物组合物的释放、癌症的治疗,及其组合。
尽管使用多个实施例来详细讨论本发明,但是说明书的记载不是用来限制本发明的。采用本领域技术人员熟知的方式做出的各种修饰和实施例的组合也属于本发明的一部分。具体的保护范围参见本发明权利要求书的记载。
序列表
<110>得克萨斯州立大学董事会(Board of Regents,the University of Texas System)
<120>包含肽结合域的组合物及由其形成纳米颗粒和纳米导线的方法
<130>PIF090431C
<140>N/A
<141>2002-09-25
<150>60/325,664
<151>2001-09-28
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<400>29
Gly Tyr His Met Gln Thr Leu Pro Gly Pro Val Ala
1 5 10
<210>30
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>30
Ser Leu Thr Pro Leu Thr Thr Ser His Leu Arg Ser
1 5 10
<210>31
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>31
Thr Leu Thr Asn Gly Pro Leu Arg Pro Phe Thr Gly
1 5 10
<210>32
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>32
Leu Asn Thr Pro Lys Pro Phe Thr Leu Gly Gln Asn
1 5 10
<210>33
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>33
Cys Asp Leu Gln Asn Tyr Lys Ala Cys
1 5
<210>34
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>34
Cys Arg His Pro His Thr Arg Leu Cys
1 5
<210>35
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>35
Cys Ala Asn Leu Lys Pro Lys Ala Cys
1 5
<210>36
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>36
Cys Tyr Ile Asn Pro Pro Lys Val Cys
1 5
<210>37
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>37
Cys Asn Asn Lys Val Pro Val Leu Cys
1 5
<210>38
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>38
Cys His Ala Ser Lys Thr Pro Leu Cys
1 5
<210>39
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>39
Cys Ala Ser Gln Leu Tyr Pro Ala Cys
1 5
<210>40
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>40
Cys Asn Met Thr Gln Tyr Pro Ala Cys
1 5
<210>41
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>41
Cys Phe Ala Pro Ser Gly Pro Ala Cys
1 5
<210>42
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>42
Cys Pro Val Trp Ile Gln Ala Pro Cys
1 5
<210>43
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>43
Cys Gln Val Ala Val Asn Pro Leu Cys
1 5
<210>44
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>44
Cys Gln Pro Glu Ala Met Pro Ala Cys
1 5
<210>45
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>45
Cys His Pro Thr Met Pro Leu Ala Cys
1 5
<210>46
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>46
Cys Pro Pro Phe Ala Ala Pro Ile Cys
1 5
<210>47
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>47
Cys Asn Lys His Gln Pro Met His Cys
1 5
<210>48
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>48
Cys Phe Pro Met Arg Ser Asn Gln Cys
1 5
<210>49
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>49
Cys Gln Ser Met Pro His Asn Arg Cys
1 5
<210>50
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>50
Cys Asn Asn Pro Met His Gln Asn Cys
1 5
<210>51
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>51
Cys His Met Ala Pro Arg Trp Gln Cys
1 5
<210>52
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>52
His Val His Ile His Ser Arg Pro Met
1 5
<210>53
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>53
Leu Pro Asn Met His Pro Leu Pro Leu
1 5
<210>54
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>54
Leu Pro Leu Arg Leu Pro Pro Met Pro
1 5
<210>55
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>55
His Ser Met Ile Gly Thr Pro Thr Thr
1 5
<210>56
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>56
Ser Val Ser Val Gly Met Lys Pro Ser
1 5
<210>57
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>57
Leu Asp Ala Ser Phe Met Gln Asp Trp
1 5
<210>58
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>58
Thr Pro Pro Ser Tyr Gln Met Ala Met
1 5
<210>59
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>59
Tyr Pro Gln Leu Val Ser Met Ser Thr
1 5
<210>60
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>60
Gly Tyr Ser Thr Ile Asn Met Tyr Ser
1 5
<210>61
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>61
Asp Arg Met Leu Leu Pro Phe Asn Leu
1 5
<210>62
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>62
Ile Pro Met Thr Pro Ser Tyr Asp Ser
1 5
<210>63
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>63
Met Tyr Ser Pro Arg Pro Pro Ala Leu
1 5
<210>64
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>64
Gln Pro Thr Thr Asp Leu Met Ala His
1 5
<210>65
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>65
Ala Thr His Val Gln Met Ala Trp Ala
1 5
<210>66
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>66
Ser Met His Ala Thr Leu Thr Pro Met
1 5
<210>67
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>67
Ser Gly Pro Ala His Gly Met Phe Ala
1 5
<210>68
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>68
Ile Ala Asn Arg Pro Tyr Ser Ala Gln
1 5
<210>69
<211>7
<212>PRT
<213>人工序列
<220>
<223>肽
<400>69
Val Met Thr Gln Pro Thr Arg
1 5
<210>70
<211>7
<212>PRT
<213>人工序列
<220>
<223>肽
<400>70
His Met Arg Pro Leu Ser Ile
1 5
<210>71
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>71
Leu Thr Arg Ser Pro Leu His Val Asp Gln Arg Arg
1 5 10
<210>72
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>72
Val Ile Ser Asn His Ala Glu Ser Ser Arg Arg Leu
1 5 10
<210>73
<211>7
<212>PRT
<213>人工序列
<220>
<223>肽
<400>73
His Thr His Ile Pro Asn Gln
1 5
<210>74
<211>7
<212>PRT
<213>人序列
<220>
<223>肽
<400>74
Leu Ala Pro Val Ser Pro Pro
1 5
<210>75
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>75
Cys Met Thr Ala Gly Lys Asn Thr Cys
1 5
<210>76
<211>9
<213>人工序列
<220>
<223>肽
<400>76
Cys Gln Thr Leu Trp Arg Asn Ser Cys
1 5
<210>77
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>77
Cys Thr Ser Val His Thr Asn Thr Cys
1 5
<210>78
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>78
Cys Pro Ser Leu Ala Met Asn Ser Cys
1 5
<210>79
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>79
Cys Ser Asn Asn Thr Val His Ala Cys
1 5
<210>80
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>80
Cys Leu Pro Ala Gln Gly His Val Cys
1 5
<210>81
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>81
Cys Leu Pro Ala Gln Val His Val Cys
1 5
<210>82
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>82
Cys Pro Pro Lys Asn Val Arg Leu Cys
1 5
<210>83
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>83
Cys Pro His Ile Asn Ala His Ala Cys
1 5
<210>84
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>84
Cys Ile Val Asn Leu Ala Arg Ala Cys
1 5
<210>85
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>85
Thr Met Gly Phe Thr Ala Pro Arg Phe Pro His Tyr
1 5 10
<210>86
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>86
Ala Thr Gln Ser Tyr Val Arg His Pro Ser Leu Gly
1 5 10
<210>87
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>87
Thr Ser Thr Thr Gln Gly Ala Leu Ala Tyr Leu Phe
1 5 10
<210>88
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>88
Asp Pro Pro Trp Ser Ala Ile Val Arg His Arg Asp
1 5 10
<210>89
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>89
Phe Asp Asn Lys Pro Phe Leu Arg Val Ala Ser Glu
1 5 10
<210>90
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>90
His Gln Ser His Thr Gln Gln Asn Lys Arg His Leu
1 5 10
<210>91
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>91
Thr Ser Thr Thr Gln Gly Ala Leu Ala Tyr Leu Phe
1 5 10
<210>92
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>92
Lys Thr Pro Ile His Thr Ser Ala Trp Glu Phe Gln
1 5 10
<210>93
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>93
Asp Leu Phe His Leu Lys Pro Val Ser Asn Glu Lys
1 5 10
<210>94
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>94
Lys Pro Phe Trp Thr Ser Ser Pro Asp Val Met Thr
1 5 10
<210>95
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>95
Pro Trp Ala Ala Thr Ser Lys Pro Pro Tyr Ser Ser
1 5 10
<210>96
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>96
Cys Gln Asn Pro Met Gln Thr Phe Cys
1 5
<210>97
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>97
Cys Asn Gln Leu Ser Thr Arg Pro Cys
1 5
<210>98
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>98
Cys Leu Gln Asn Arg Gln Ser Gln Cys
1 5
<210>99
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>99
Cys Gln Leu Gln Arg Gln Trp Asn Cys
1 5
<210>100
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>100
Cys Gln Val Asn Ser Ala His Gln Cys
1 5
<210>101
<211>9
<212>P RT
<213>人工序列
<220>
<223>肽
<400>101
Cys Phe Pro Met Arg Ser Asn Gln Cys
1 5
<210>102
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>102
Cys Pro Pro Gln Pro Asn Arg Gln Cys
1 5
<210>103
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>103
Cys Gln Met Pro Met Gln His Asn Cys
1 5
<210>104
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>104
Cys Ala Asn Val Ala Gln Arg Asn Cys
1 5
<210>105
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>105
Cys Asn Asn Lys Gln Leu Tyr Tyr Cys
1 5
<210>106
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>106
Cys Gln Thr Ala Trp Ile Gly Gln Cys
1 5
<210>107
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>107
Cys Gln Ser Ala Asn Lys Leu Thr Cys
1 5
<210>108
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>108
Cys Ile Pro Tyr Thr Met Ala Met Cys
1 5
<210>109
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>109
Cys Leu Pro Ser Tyr His Asn Asn Cys
1 5
<210>110
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>110
Cys Val Ser Val Ala His Lys Asp Cys
1 5
<210>111
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>111
Cys Glu Val Thr Thr Leu Tyr Arg Cys
1 5
<210>112
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>112
Cys Glu Leu Thr Ala Phe Pro Ala Cys
1 5
<210>113
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>113
Cys Thr Leu Ala Ser Pro His Gln Cys
1 5
<210>114
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>114
Cys Pro Leu Thr Gly Gly Pro Thr Cys
1 5
<210>115
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>115
Cys Trp Trp Ser Trp His Pro Trp Cys
1 5
<210>116
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>116
Cys Gln Lys Ser Gly Val His Leu Cys
1 5
<210>117
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>117
Cys Leu Phe Asn Ala Leu Ile Arg Cys
1 5
<210>118
<21l>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>118
Cys Val Met Trp Thr Ser His Ser Cys
1 5
<210>119
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>119
Cys Val Ser Arg Trp Arg Ala Ser Cys
1 5
<210>120
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>120
Cys Ser Ser Trp Glu Pro Lys Ser Cys
1 5
<210>121
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>121
Cys Thr Leu Thr Gly Pro Phe Ala Cys
1 5
<210>122
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>122
Cys Pro Pro Val Leu Gly Asn Leu Cys
1 5
<210>123
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>123
Cys Pro His Ala Pro Ser Gly Pro Cys
1 5
<210>124
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>124
Cys Pro Leu His Lys Asn Gly Lys Cys
1 5
<210>125
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>125
Cys Arg Ser His His Ser Trp Ser Cys
1 5
<210>126
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>126
Cys Lys Gln Phe Leu Ser Leu Ser Cys
1 5
<210>127
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>127
Cys Asp Asp Ala Ser Leu Arg His Cys
1 5
<210>128
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>128
Cys Asp Asn Arg Gly Ser Gln Phe Cys
1 5
<210>129
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>129
Cys His His Asn Leu Ser Ser Ala Cys
1 5
<210>130
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>130
Cys Ile Thr Gly Pro Thr Gly Ala Cys
1 5
<210>131
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>131
Cys Pro Pro Gly Pro Thr Ala Ser Cys
1 5
<210>132
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>132
Cys His Gln Ala Gly Gly His Gln Cys
1 5
<210>133
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>133
Cys Tyr Phe Ser Trp Trp His Pro Cys
1 5
<210>134
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>134
Cys Ser Pro Val Lys Tyr Pro Ser Cys
1 5
<210>135
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>135
Cys Thr Ser His Phe Lys Leu His Cys
1 5
<210>136
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>136
Cys Gln Gln Gly Thr Ala Pro Leu Cys
1 5
<210>137
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>137
Cys Gln Glu His Ser Ala Lys Ser Cys
1 5
<210>138
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>138
Cys Gln Thr Glu Asp Leu Pro Arg Cys
1 5
<210>139
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>139
Cys Asn Arg Thr Ser Pro Ala His Cys
1 5
<210>140
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>140
Cys Gln Gly Asn His Ile Gly Leu Cys
1 5
<210>141
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>141
Cys Leu Asn Asn Tyr Thr His Thr Cys
1 5
<210>142
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>142
Cys Leu Thr Thr Ala Ser Thr Lys Cys
1 5
<210>143
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>143
Cys Leu Leu Ser Leu Arg Pro Ala Cys
1 5
<210>144
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>144
Cys Asp Ser Gln Leu Trp Pro Ile Cys
1 5
<210>145
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>145
Cys Asp Asp Arg Thr Thr Lys Ile Cys
1 5
<210>146
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>146
Cys Trp Trp Pro Asp Gly Trp Tyr Cys
1 5
<210>147
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>147
Cys Lys Leu Gln Leu Thr Asn Gln Cys
1 5
<210>148
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>148
Cys Trp His Gly Leu Gly Gly Asn Cys
1 5
<210>149
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>149
Cys His Ile Thr Leu Leu Lys Arg Cys
1 5
<210>150
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>150
Cys Glu Ser Met Ala Arg Pro His Cys
1 5
<210>151
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>151
Cys His Trp Ser Trp Trp His Pro Cys
1 5
<210>152
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>152
Cys Thr Leu Leu Leu Ser Arg Asn Cys
1 5
<210>153
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>153
Cys Ser Ser Val Ser Tyr Met Ala Cys
1 5
<210>154
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>154
Cys His Trp Arg Trp Leu Pro Ala Cys
1 5
<210>155
<211>11
<212>PRT
<213>人工序列
<220>
<223>肽
<400>155
Trp Ser Pro Gly Gln Gln Arg Leu His Asn Ser Xaa
1 5 10
<210>156
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<220>
<221>misc_feature
<222>(12)..(12)
<223>X=any amino acid
<400>156
Asp Ser Ser Asn Pro Ile Phe Trp Arg Pro Ser Ser
1 5 10
<210>157
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>157
Glu Pro Phe Pro Ala Ser Ser Leu Met Thr Ile Arg
1 5 10
<210>158
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>158
Ser Tyr His Trp Asp Lys Thr Pro Gln Val Leu Ile
1 5 10
<210>159
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>159
Ser Gly His Gln Leu Leu Leu Asn Lys Met Pro Asn
1 5 10
<210>160
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>160
Ser Ile Pro Ser Glu Ala Ser Leu Ser Ser Pro Arg
1 5 10
<210>161
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>161
Thr Val Pro Pro Gln Leu Asn Ala Gln Phe Arg Ser
1 5 10
<210>162
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>162
Ser Asp Asn Val His Thr Trp Gln Ala Met Phe Lys
1 5 10
<210>163
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>163
Tyr Pro Ser Leu Leu Lys Met Gln Pro Gln Phe Ser
1 5 10
<210>164
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>164
Leu Pro Ile Pro Ala His Val Ala Pro His Gly Pro
1 5 10
<210>165
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>165
Leu Trp Gly Arg Pro Phe Pro Asp Leu Leu His Gln
1 5 10
<210>166
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>166
Gln Thr Pro Pro Trp Ile Leu Ser His Pro Pro Gln
1 5 10
<210>167
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>167
Asn His Pro His Pro Thr Pro Ala Arg Gly Ile Ile
1 5 10
<210>168
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>168
His Pro Ser Ser Ala Pro Trp Gly Val Ala Leu Ala
1 5 10
<210>169
<211>11
<212>PRT
<213>人工序列
<220>
<223>肽
<400>169
His Trp Asn His Arg Tyr Ser Met Trp Gly Ala
1 5 10
<210>170
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>170
Asn His Arg Ile Trp Glu Ser Phe Trp Pro Ser Ala
1 5 10
<210>171
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>171
His Ser Ser Trp Trp Leu Ala Leu Ala Lys Pro Thr
1 5 10
<210>172
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>172
Ser Asn Asn Asp Leu Ser Pro Leu Gln Thr Ser His
1 5 10
<210>173
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>173
Ser Gly Leu Pro His Leu Ser Leu Asn Ala Pro Arg
1 5 10
<210>174
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>174
Ser Trp Pro Leu Tyr Ser Arg Asp Ser Gly Leu Gly
1 5 10
<210>175
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>175
Leu Pro Gly Trp Pro Leu Ala Glu Arg Val Gly Gln
1 5 10
<210>176
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>176
Ser His Pro Trp Asn Ala Gln Arg Glu Leu Ser Val
1 5 10
<210>177
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>177
Val Ser Arg His Gln Ser Trp His Pro His Asp Leu
1 5 10
<210>178
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>178
Tyr Trp Pro Ser Lys His Trp Trp Trp Leu Ala Pro
1 5 10
<210>179
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>179
Ser Ser Ala Trp Trp Ser Tyr Trp Pro Pro Val Ala
1 5 10
<210>180
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>180
Ala Pro Leu Gly Phe Asn Ser Met Arg Leu Pro Ala
1 5 10
<210>181
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>181
Trp Asn Met Arg Trp Leu Pro Thr Trp Ala Pro Ala
1 5 10
<210>182
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>182
Trp Pro Arg Tyr Pro Ser Thr Leu Val Ser Ser His
1 5 10
<210>183
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>183
Gly Lys Glu Ser Val Pro Pro Pro Arg Ile Tyr Ala
1 5 10
<210>184
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>184
Leu Thr Leu Asp Met Lys Arg Thr Ser Gly Pro Leu
1 5 10
<210>185
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>185
Leu Ser Thr His Thr Thr Glu Ser Arg Ser Met Val
1 5 10
<210>186
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>186
Glu Tyr Leu Ser Ala Ile Val Ala Gly Pro Trp Pro
1 5 10
<210>187
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>187
Gln Phe Lys Trp Trp His Ser Leu Ser Pro Thr Pro
1 5 10
<210>188
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>188
Ala Pro Thr Pro Leu Ile Gly Lys Arg Leu Val Gln
1 5 10
<210>189
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>189
Leu Ile Asn Pro Arg Asp His Val Leu Ala Pro Gln
1 5 10
<210>190
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>190
Leu Leu Ala Asp Thr Thr His His Arg Pro Trp Thr
1 5 10
<210>191
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>191
Gln Ala Ser Ile Ser Pro Leu Trp Thr Pro Thr Pro
1 5 10
<210>192
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<220>
<221>misc_feature
<222>(3)..(3)
<223>X=任意氨基酸
<400>192
Asn Ser Xaa Leu His Leu Ala His Gln Pro His Lys
1 5 10
<210>193
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>193
Thr Lys Asn Met Leu Ser Leu Pro Val Gly Pro Gly
1 5 10
<210>194
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>194
Asp Met Pro Arg Thr Thr Met Ser Pro Pro Pro Arg
1 5 10
<210>195
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>195
Ser Thr Pro Ala Leu Met Thr Leu Ile Ala Arg Thr
1 5 10
<210>196
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>196
Thr Ser Asn Phe Ile Asn Arg Met Asn Pro Gly Leu
1 5 10
<210>197
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>197
Thr Ser Ala Ser Thr Arg Pro Glu Leu His Tyr Pro
1 5 10
<210>198
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>198
Asn Leu Leu Glu Val Ile Ser Leu Pro His Arg Gly
1 5 10
<210>199
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>199
Gln His Pro Asn Asn Ala His Val Arg Gln Phe Pro
1 5 10
<210>200
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>200
Gln His Ala Asn Asn Gln Ala Trp Asn Asn Leu Arg
1 5 10
<210>201
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>201
Gln His Tyr Pro Gly Arg Ala Ile Pro His Ser Thr
1 5 10
<210>202
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>202
Val Pro Pro Pro His Pro Gln Phe Asp His Leu Ile
1 5 10
<210>203
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>203
Leu Lys Met Asn Pro Ser Ile Ser Ser Ser Leu Lys
1 5 10
<210>204
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>204
His Trp Asp Pro Phe Ser Leu Ser Ala Tyr Phe Pro
1 5 10
<210>205
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>205
Trp Ser Pro Gly Gln Gln Arg Leu His Asn Ser Thr
1 5 10
<210>206
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>206
Asn Met Thr Lys His Pro Leu Ala Tyr Thr Glu Pro
1 5 10
<210>207
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>207
His Met Pro Thr Lys Ser Ala Ser Gln Thr Tyr Phe
1 5 10
<210>208
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>208
His Asn Ala Tyr Trp His Trp Pro Pro Ser Met Thr
1 5 10
<210>209
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>209
Val Leu Pro Pro Lys Pro Met Arg Gln Pro Val Ala
1 5 10
<210>210
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>210
Ser Leu His Lys Ile Ser Gln Leu Ser Phe Ala Ser
1 5 10
<210>211
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>211
Trp His Ser Arg Leu Pro Pro Met Thr Val Ala Phe
1 5 10
<210>212
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>212
Thr Pro Trp Phe Gln Trp His Gln Trp Asn Leu Asn
1 5 10
<210>213
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>213
Ser Asp Thr Ile Ser Arg Leu His Val Ser Met Thr
1 5 10
<210>214
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>214
Asn Pro Tyr His Pro Thr Ile Pro Gln Ser Val His
1 5 10
<210>215
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>215
Leu Pro Ser Ala Lys Leu Pro Pro Gly Pro Pro Lys
1 5 10
<210>216
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>216
Thr Ser Asn Pro His Thr Arg His Tyr Tyr Pro Ile
1 5 10
<210>217
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>217
Ser Asn Phe Thr Thr Gln Met Thr Phe Tyr Thr Gly
1 5 10
<210>218
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>218
Lys Met Asp Arg His Asp Pro Ser Pro Ala Leu Leu
1 5 10
<210>219
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>219
Met Pro Ala Val Met Ser Ser Ala Gln Val Pro Arg
1 5 10
<210>220
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>220
Asp Arg Ala Pro Leu Ile Pro Phe Ala Ser Gln His
1 5 10
<210>221
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>221
Asp Gln Tyr Ile Gln Gln Ala His Arg Ser His Ile
1 5 10
<210>222
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>222
His Ala Arg Ile Asn Pro Ser Phe Pro Leu Pro Ile
1 5 10
<210>223
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>223
Gly Trp Trp Pro Tyr Ala Ala Leu Arg Ala Leu Ser
1 5 10
<210>224
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>224
Thr Ala Ala Thr Ser Ser Pro His Ser Arg Ser Pro
1 5 10
<210>225
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>225
Ser Thr Thr Gly Gln Ser Pro Ala Leu Ala Pro Pro
1 5 10
<210>226
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>226
His Ser Ser Trp Tyr Ile Gln His Phe Pro Pro Leu
1 5 10
<210>227
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>227
Gly Ser His Ser Asn Pro Thr Pro Leu Thr Pro Arg
1 5 10
<210>228
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>228
Tyr Thr Gly Val Leu Asp Thr Lys Ala Thr Gln Asn
1 5 10
<210>229
<211>7
<212>PRT
<213>人工序列
<220>
<223>肽
<400>229
Asn Asn Pro His Met Gln Asn
1 5
<210>230
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>230
Val Ile Ser Asn His Ala Glu Ser Ser Arg Arg Leu
1 5 10
<210>231
<211>7
<212>PRT
<213>人工序列
<220>
<223>肽
<400>231
Asp Ser Pro His Arg His Ser
1 5
<210>232
<211>8
<212>PRT
<213>人工序列
<220>
<223>肽
<400>232
Asn Asn Pro Met His Gln Asn Cys
1 5
<210>233
<211>10
<212>PRT
<213>人工序列
<220>
<223>肽
<400>233
Ser Gly Pro Ala His Gly Met Phe Ala Arg
1 5 10
<210>234
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>234
Cys Thr Tyr Ser Arg Leu His Leu Cys
1 5
<210>235
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>235
Cys Arg Pro Tyr Asn Ile His Gln Cys
1 5
<210>236
<211>9
<212>PRT
<213>人工序列
<220>
<223>肽
<400>236
Cys Pro Phe Lys Thr Ala Phe Pro Cys
1 5
<210>237
<211>7
<212>PRT
<213>人工序列
<220>
<223>肽
<220>
<221>misc_feature
<222>(1)..(2)
<223>X=N or Q
<220>
<221>misc_feature
<222>(6)..(7)
<223>X=N or Q
<400>237
Xaa Xaa Pro Met His Xaa Xaa
1 5
<210>238
<211>7
<212>PRT
<213>人工序列
<220>
<223>肽
<400>238
Trp Trp Ser Trp His Pro Trp
1 5
<210>239
<211>7
<212>PRT
<213>人工序列
<220>
<223>肽
<400>239
His Trp Ser Trp Trp His Pro
1 5
<210>240
<211>14
<212>PRT
<213>人工序列
<220>
<223>肽
<400>240
Ala Cys Trp Trp Ser Trp His Pro Trp Cys Gly Gly Gly Lys
1 5 10
<210>241
<211>14
<212>PRT
<213>人工序列
<220>
<223>肽
<400>241
Ala Cys Asp Ser Pro His Arg His Ser Cys Gly Gly Gly Lys
1 5 10
<210>242
<211>14
<212>PRT
<213>人工序列
<220>
<223>肽
<400>242
Ala Cys Pro Arg Ser Ser His Asp His Cys Gly Gly Gly Lys
1 5 10
<210>243
<211>7
<212>PRT
<213>人工序列
<220>
<223>肽
<400>243
Tyr Phe Ser Trp Trp His Pro
1 5
<210>244
<211>16
<212>PRT
<213>人工序列
<220>
<223>肽
<400>244
Asp Met Pro Arg Thr Thr Met Ser Pro Pro Pro Arg Gly Gly Gly Lys
1 5 10 15
<210>245
<211>12
<212>PRT
<213>人工序列
<220>
<223>肽
<400>245
Asn His Arg Ile Trp Glu Ser Phe Trp Pro Ser Ala 。
1 5 10
Claims (10)
1.包括一种或多种肽结合域的组合物,其特征在于所述结合域选择性地与无机靶晶体组合物结合或与无机靶晶体组合物的晶面结合,该结合域选择性地使靶晶体组合物的纳米颗粒成核。
2.根据权利要求1所述的组合物,其特征在于所述组合物进一步包括一个或多个与结合域相结合的无机靶晶体组合物的纳米颗粒。
3.根据权利要求1所述的组合物,其特征在于所述无机靶晶体组合物包括金属或金属的氧化物。
4.包括一种或多种肽结合域的组合物,其特征在于所述结合域选择性地与包含Ba,Sr,Ti,Bi,Ta,Zr,Fe,Ni,Mn,Pb,La,Li,Na,K,Rb,Cs,Fr,Be,Mg,Ca,Nb,Tl,Hg,Cu,Co,Rh,Sc,Y或其组合的靶物质结合。
5.根据权利要求1所述的组合物,其特征在于所述结合域是通过噬菌体淘洗而筛选的。
6.根据权利要求1所述的组合物,其特征在于所述结合域选自肽文库。
7.一种形成纳米颗粒的方法,其特征在于所述方法包括将权利要求1的组合物与纳米颗粒前体物相接触从而形成纳米颗粒的步骤。
8.一种形成纳米导线的方法,其特征在于所述方法包括将权利要求1的组合物与纳米颗粒前体物相接触从而形成纳米颗粒的步骤,该纳米颗粒与所述组合物相结合并以纳米导线的形式取向排列。
9.一种形成纳米导线的方法,其特征在于所述方法包括将权利要求1的组合物与纳米颗粒相接触从而形成纳米颗粒的步骤,该纳米颗粒与所述组合物相结合且以纳米导线的形式取向排列。
10.根据权利要求7所述的方法,其中所述纳米颗粒包括金属或金属的氧化物。
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US32566401P | 2001-09-28 | 2001-09-28 | |
US60/325,664 | 2001-09-28 |
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CNA2009100081741A Pending CN101565858A (zh) | 2001-09-28 | 2002-09-27 | 包含肽结合域的组合物及由其形成纳米颗粒和纳米导线的方法 |
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US (2) | US20030113714A1 (zh) |
EP (1) | EP1432527A4 (zh) |
JP (1) | JP2005505915A (zh) |
KR (1) | KR100942320B1 (zh) |
CN (2) | CN100479930C (zh) |
AU (1) | AU2002343464B2 (zh) |
CA (1) | CA2461898A1 (zh) |
HK (1) | HK1085689A1 (zh) |
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US20030148380A1 (en) * | 2001-06-05 | 2003-08-07 | Belcher Angela M. | Molecular recognition of materials |
US20050164515A9 (en) * | 2001-06-05 | 2005-07-28 | Belcher Angela M. | Biological control of nanoparticle nucleation, shape and crystal phase |
US20030113714A1 (en) * | 2001-09-28 | 2003-06-19 | Belcher Angela M. | Biological control of nanoparticles |
US6670179B1 (en) * | 2001-08-01 | 2003-12-30 | University Of Kentucky Research Foundation | Molecular functionalization of carbon nanotubes and use as substrates for neuronal growth |
US8865347B2 (en) * | 2001-09-28 | 2014-10-21 | Siluria Technologies, Inc. | Digital alloys and methods for forming the same |
US20030073104A1 (en) * | 2001-10-02 | 2003-04-17 | Belcher Angela M. | Nanoscaling ordering of hybrid materials using genetically engineered mesoscale virus |
AU2003213246A1 (en) * | 2002-02-21 | 2003-09-09 | University Of Virginia Patent Foundation | Bone targeting peptides |
US20060035223A1 (en) * | 2002-03-13 | 2006-02-16 | Naik Rajesh R | Method of isolating binding peptides from a combinatorial phage display library and peptides produced thereby |
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KR20040047864A (ko) | 2004-06-05 |
WO2003026590A2 (en) | 2003-04-03 |
WO2003026590A3 (en) | 2003-12-04 |
CN1744954A (zh) | 2006-03-08 |
EP1432527A2 (en) | 2004-06-30 |
US20030113714A1 (en) | 2003-06-19 |
JP2005505915A (ja) | 2005-02-24 |
US20120003629A9 (en) | 2012-01-05 |
CA2461898A1 (en) | 2003-04-03 |
CN100479930C (zh) | 2009-04-22 |
US20060275791A1 (en) | 2006-12-07 |
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