CN108137814B - 模压成形体和模压成形体的制造方法 - Google Patents
模压成形体和模压成形体的制造方法 Download PDFInfo
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Abstract
本发明提供一种模压成形体，其为包含多肽的组合物的模压成形体，所述多肽为选自由天然蛛丝蛋白和来源于天然蛛丝蛋白的多肽组成的组中的至少一种。
Description
技术领域
本发明涉及模压成形体和模压成形体的制造方法。
背景技术
以轻量化、削减成本、成形加工的容易化等为目的，进行了用有机材料代替金属材料的尝试。作为这样的有机材料，多使用树脂中硬度高的酚醛树脂，为了进一步提高弯曲弹性模量和弯曲强度，已知有在含有酚醛树脂的基体树脂中添加酚醛树脂纤维的方法(例如参考专利文献1)。另外，由于环境保护意识的提高，作为非石油资源材料的生物塑料从以前就受到关注，已知通过将蚕丝粉树脂化可得到弯曲弹性模量为4.5GPa的成形体(例如参考非专利文献1)。
现有技术文献
专利文献
专利文献1：日本特开2014-80491号公报
非专利文献
非专利文献1：平井伸治、月刊機能材料誌(月刊功能材料杂志)、2014年6月、“廃棄物由来動物タンパク質を用いた環境調和型シルクおよび羊毛樹脂(使用了废弃物来源动物蛋白的环境友好型蚕丝和羊毛树脂)”
发明内容
发明所要解决的问题
但是，专利文献1中公开的材料是通过含有纤维而发挥增强效果的材料，凭基体树脂本身难以得到高强度。另外，无法利用生物分解性材料得到弯曲弹性模量大于4.5GPa的成形体。
因此，本发明的目的在于，提供即使不使用强化纤维等添加材料也发挥出优良的弯曲弹性模量的生物分解性成形体及其制造方法。
用于解决问题的方法
本发明提供一种模压成形体，其为包含多肽的组合物的模压成形体，上述多肽为选自由天然蛛丝蛋白和来源于天然蛛丝蛋白的多肽组成的组中的至少一种。
上述成形体具有生物分解性，并且特征在于以天然蛛丝蛋白和/或来源于天然蛛丝蛋白的多肽蛋白质作为原料，而且是将该原料模压成形而得到的，基于这些特征，即使不使用强化纤维等添加材料，也发挥出非常高的弯曲弹性模量(例如大于4.5GPa)。进一步，还能够对成形体赋予透明性，因此与酚醛树脂、聚醚醚酮(PEEK)等虽为高强度但缺乏透明性的树脂相比，具有可应用的用途显著增加这样的优点。此外，蛛丝蛋白可以进行各种基因改造，因此能够容易地根据最终用途实现性能的优化。需要说明的是，弯曲弹性模量优选为4.7GPa以上，更优选为5.0GPa以上，进一步优选为5.2GPa以上。对于弯曲弹性模量的上限没有限制，例如可以设定为15.0GPa以下。弯曲弹性模量可以设定为10.0GPa以下，进而可以设定为7.0GPa以下。
上述模压成形体可以以加热加压成形体的形式提供。模压成形体是指利用铸模(mold)进行成形而得到的成形体等，通过进行加热和加压，形成弯曲弹性模量更优良的成形体。
上述模压成形体可以通过具备对包含选自由天然蛛丝蛋白和来源于天然蛛丝蛋白的多肽组成的组中的至少一种的组合物进行加热和加压的工序的制造方法来制造。
发明效果
根据本发明，能够提供即使不使用强化纤维等添加材料也发挥出优良的弯曲弹性模量的生物分解性成形体及其制造方法。
附图说明
图1是加压成形机的示意截面图。
图2(a)是组合物导入前的加压成形机的示意截面图，图2(b)是组合物刚导入后的加压成形机的示意截面图，图2(c)是对组合物进行加热和加压的状态的加压成形机的示意截面图。
图3是实施例1的模压成形体的照片。
具体实施方式
以下，对本发明的优选实施方式进行说明。但是，本发明不受下述实施方式的任何限定。
实施方式的模压成形体由包含天然蛛丝蛋白和/或来源于天然蛛丝蛋白的多肽的组合物构成。模压成形体可以通过将上述组合物导入至铸模(mold)中进行成形加工等而得到，在成形加工工序中，可以进行加热和/或加压。组合物典型地具有粉末状(冷冻干燥粉末等)或纤维状(纺丝得到的纤维等)的形状，模压成形体可以为包含这种形状的天然蛛丝蛋白和/或来源于天然蛛丝蛋白的多肽的组合物的熔合体。
作为天然蛛丝蛋白，可以列举例如大吐丝管牵引丝蛋白、横丝蛋白。
大吐丝管牵引丝蛋白是由蜘蛛的大壶状腺产生的蛋白质，具有强韧性优良的特征。作为大吐丝管牵引丝蛋白，可以列举来源于金纺蜘蛛(Nephila clavipes)的大壶状腺丝蛋白MaSp1、MaSp2、来源于十字园蛛(Araneus diadematus)的ADF3、ADF4等。
作为横丝蛋白，是由蜘蛛的鞭状腺(flagelliform gland)产生的蛋白质，作为横丝蛋白，包含例如来源于金纺蜘蛛(Nephila clavipes)的鞭毛状丝蛋白(flagelliformsilk protein)。
作为来源于天然蛛丝蛋白的多肽，可以列举重组蛛丝蛋白、例如天然型蛛丝蛋白的突变体、类似物或衍生物等。作为这样的多肽，特别优选大吐丝管牵引丝蛋白的重组蛛丝蛋白。
模压成形体可以仅为天然蛛丝蛋白和/或来源于天然蛛丝蛋白的多肽(以下，有时将它们合并统称为“蛛丝多肽”)的模压成形体，也可以是在蛛丝多肽中添加有添加成分(例如增塑剂、着色剂、层状硅酸盐或碱性磷酸钙等填料、水分、合成树脂等)的物质的模压成形体。在使用增塑剂等添加成分的情况下，优选使其为蛛丝多肽的合计量的50质量％以下。另外，可以含有其他蛋白、例如蚕丝丝心蛋白、大豆蛋白、酪蛋白、角蛋白、胶原蛋白、乳清蛋白或在获得多肽的过程中生成的夹杂物。需要说明的是，模压成形体即使在不含有上述添加成分的情况下也发挥本发明的效果。
蛛丝多肽的模压成形体优选具有透明性。透明性可以通过目视进行判断，但优选在使用光学透射率测定器在例如220～800nm的波长范围内使累积时间为0.1秒钟的情况下，透射率为50％以上的模压成形体。
模压成形体可以使用加压成形机来制作。图1是能够用于制造模压成形体的加压成形机的示意截面图。图1所示的加压成形机10具备形成有贯通孔且可进行加热的模具2、以及能够在模具2的贯通孔内上下移动的上侧销4和下侧销6，在向模具2中插入上侧销4或下侧销6而产生的空隙内导入包含蛛丝多肽的组合物，一边对模具2进行加热，一边利用上侧销4和下侧销6对组合物进行压缩，由此能够得到模压成形体。
图2是示出得到模压成形体的工序图，图2(a)是组合物导入前的加压成形机的示意截面图，图2(b)是组合物刚导入后的加压成形机的示意截面图，图2(c)是对组合物进行加热和加压的状态的加压成形机的示意截面图。如图2(a)所示，在模具2的贯通孔中仅插入有下侧销6的状态下向贯通孔内导入组合物，如图2(b)所示，向模具2的贯通孔中插入上侧销4并使其下降，开始模具2的加热，在贯通孔内对加热加压前的组合物8a进行加热加压。使上侧销4下降至达到预先规定的加压力为止，在图2(c)所示的状态下继续加热和加压直至组合物达到规定的温度为止，得到加热加压后的组合物8b。然后，使用冷却器(例如点式制冷机)使模具2的温度下降，在组合物8b达到规定的温度时，从模具2中拔出上侧销4或下侧销6，取出内容物，得到模压成形体。关于加压，可以在将下侧销6固定的状态下使上侧销4下降来实施，也可以实施上侧销4的下降和下侧销6的升高这两者。
加热优选在80～300℃下进行，更优选为100～180℃，进一步优选为100～130℃。加压优选以5kN以上进行，更优选为10kN以上，进一步优选为20kN以上。另外，在达到规定的加热加压条件后，在该条件下继续处理的时间(保温条件)优选为0～100分钟，更优选为1～50分钟，进一步优选为5～30分钟。
包含蛛丝多肽的组合物的模压成形体优选使用来源于天然蛛丝蛋白的多肽来制作，因此以下对该制造方法进行详述。
作为成为包含蛛丝多肽的组合物的模压成形体的原料的来源于大吐丝管牵引丝蛋白的多肽，可以列举包含2个以上、优选5个以上、更优选10个以上的式1：REP1-REP2(1)所示的氨基酸序列单元的多肽。或者，来源于大吐丝管牵引丝蛋白的多肽可以是包含式1：REP1-REP2(1)所示的氨基酸序列单元、且C末端序列为序列号1～3中任意一个序列所示的氨基酸序列或与序列号1～3中任意一个序列所示的氨基酸序列具有90％以上的同源性的氨基酸序列的多肽。需要说明的是，来源于大吐丝管牵引丝蛋白的多肽中，式1：REP1-REP2(1)所示的氨基酸序列单元可以相同，也可以不同。关于上述来源于大吐丝管牵引丝蛋白的多肽，在进行以大肠杆菌等微生物为宿主的重组蛋白生产的情况下，从生产率的观点出发，优选分子量为500kDa以下，更优选为300kDa以下，进一步优选为200kDa以下。
式1中，REP1是指聚丙氨酸。REP1中，连续排列的丙氨酸优选为2个残基以上，更优选为3个残基以上，进一步优选为4个残基以上，特别优选为5个残基以上。另外，REP1中，连续排列的丙氨酸优选为20个残基以下，更优选为16个残基以下，进一步优选为12个残基以下，特别优选为10个残基以下。式1中，REP2为由10～200个残基的氨基酸构成的氨基酸序列，氨基酸序列中所含的甘氨酸、丝氨酸、谷氨酰胺和丙氨酸的合计残基数相对于全部氨基酸残基数为40％以上、优选为60％以上、更优选为70％以上。
大吐丝管牵引丝中，REP1相当于在纤维内形成结晶β折叠的结晶区域，REP2相当于在纤维内更具有柔软性且大部分缺乏有序结构的无定型区域。而且，[REP1-REP2]相当于由结晶区域和无定型区域构成的重复区域(重复序列)，是牵引丝蛋白的特征性序列。
序列号1所示的氨基酸序列与由ADF3的氨基酸序列(NCBI登录号：AAC47010、GI：1263287)的C末端的50个残基的氨基酸构成的氨基酸序列相同，序列号2所示的氨基酸序列与从序列号1所示的氨基酸序列的C末端去除20个残基后得到的氨基酸序列相同，序列号3所示的氨基酸序列与从序列号1所示的氨基酸序列的C末端去除29个残基后得到的氨基酸序列相同。
作为包含2个以上的式1：REP1-REP2(1)所示的氨基酸序列单元的多肽，可以使用例如由序列号7所示的氨基酸序列构成的多肽。由序列号7所示的氨基酸序列构成的多肽是在N末端附加有由起始密码子、His10标签和HRV3C蛋白酶(人鼻病毒(Human rhinovirus)3C蛋白酶)识别位点构成的氨基酸序列(序列号4)的ADF3的氨基酸序列(NCBI登录号：AAC47010、GI：1263287)中以在第543位氨基酸残基处终止翻译的方式发生了突变的多肽。
另外，作为包含2个以上的式1：REP1-REP2(1)所示的氨基酸序列单元的多肽，可以使用由在序列号7所示的氨基酸序列中置换、缺失、插入和/或添加一个或多个氨基酸而得到的氨基酸序列构成、具有由结晶区域和无定型区域构成的重复区域的蛋白质。本发明中，“一个或多个”是指例如1～40个、1～35个、1～30个、1～25个、1～20个、1～15个、1～10个或者一个或几个。另外，本发明中，“一个或几个”是指1～9个、1～8个、1～7个、1～6个、1～5个、1～4个、1～3个、1～2个或1个。
另外，作为包含2个以上的式1：REP1-REP2(1)所示的氨基酸序列单元的多肽，可以列举例如具有序列号8所示的氨基酸序列的ADF4来源的重组蛋白。序列号8所示的氨基酸序列是在由NCBI数据库获得的ADF4的部分氨基酸序列(NCBI登录号：AAC47011、GI：1263289)的N末端附加有由起始密码子、His10标签和HRV3C蛋白酶(人鼻病毒3C蛋白酶)识别位点构成的氨基酸序列(序列号4)的氨基酸序列。另外，作为包含2个以上的式1：REP1-REP2(1)所示的氨基酸序列单元的多肽，也可以使用由在序列号8所示的氨基酸序列中置换、缺失、插入和/或添加一个或多个氨基酸而得到的氨基酸序列构成、具有由结晶区域和无定型区域构成的重复区域的多肽。另外，作为包含2个以上的式1：REP1-REP2(1)所示的氨基酸序列单元的多肽，可以列举例如具有序列号9所示的氨基酸序列的MaSp2来源的重组蛋白。序列号9所示的氨基酸序列是在由NCBI数据库获得的MaSp2的部分序列(NCBI登录号：AAT75313、GI：50363147)的N末端附加有由起始密码子、His10标签和HRV3C蛋白酶(人鼻病毒3C蛋白酶)识别位点构成的氨基酸序列的氨基酸序列。另外，作为包含2个以上的式1：REP1-REP2(1)所示的氨基酸序列单元的多肽，也可以使用由在序列号9所示的氨基酸序列中置换、缺失、插入和/或添加一个或多个氨基酸而得到的氨基酸序列构成、具有由结晶区域和无定型区域构成的重复区域的多肽。
作为来源于横丝蛋白的多肽，可以列举包含10个以上、优选20个以上、更优选30个以上的式2：REP3(2)所示的氨基酸序列单元的多肽。关于来源于横丝蛋白的多肽，在进行以大肠杆菌等微生物为宿主的重组蛋白生产的情况下，从生产率的观点出发，优选分子量为500kDa以下，更优选为300kDa以下，进一步优选为200kDa以下。
式(2)中，REP3是指由Gly-Pro-Gly-Gly-X构成的氨基酸序列，X是指选自由Ala、Ser、Tyr和Val组成的组中的一种氨基酸。
蛛丝中，横丝的一大特征在于，不具有结晶区域，而具有由无定形区域构成的重复区域。推测大吐丝管牵引丝等中由于具有由结晶区域和无定形区域构成的重复区域，因而兼具高的应力和伸缩性。另一方面，与大吐丝管牵引丝相比，横丝的应力差，但具有高伸缩性。认为这是由于横丝的大部分由无定形区域构成的缘故。
作为包含10个以上的式2：REP3(2)所示的氨基酸序列单元的多肽，可以列举例如具有序列号10所示的氨基酸序列的鞭毛状丝蛋白来源的重组蛋白。序列号10所示的氨基酸序列是将由NCBI数据库获得的金纺蜘蛛的鞭毛状丝蛋白的部分序列(NCBI登录号：AAF36090、GI：7106224)的与重复部分和基序相当的N末端起第1220位残基至第1659位残基为止的氨基酸序列(记作PR1序列)与由NCBI数据库获得的金纺蜘蛛的鞭毛状丝蛋白的部分序列(NCBI登录号：AAC38847、GI：2833649)的C末端起第816位残基至第907位残基为止的C末端氨基酸序列结合，并在结合而成的序列的N末端附加由起始密码子、His10标签和HRV3C蛋白酶识别位点构成的氨基酸序列(序列号4)而得到的氨基酸序列。另外，作为包含10个以上的式2：REP3(2)所示的氨基酸序列单元的多肽，也可以使用由在序列号10所示的氨基酸序列中置换、缺失、插入和/或添加一个或多个氨基酸而得到的氨基酸序列构成、具有由无定形区域构成的重复区域的多肽。
多肽可以使用利用含有编码多肽的基因的表达载体进行了转化的宿主来制造。基因的制造方法没有特别限制，由蜘蛛来源的细胞利用聚合酶链式反应(PCR)等对编码天然型蛛丝蛋白的基因进行扩增、克隆，或者以化学方式进行合成。基因的化学合成方法也没有特别限制，例如可以基于由NCBI网络数据库等获得的天然型蛛丝蛋白的氨基酸序列信息，通过PCR等将利用AKTAoligopilot plus 10/100(通用电气医疗日本株式会社)等自动合成的寡核苷酸连接而合成。此时，为了易于进行蛋白质的纯化和确认，可以合成编码在上述氨基酸序列的N末端附加有由起始密码子和His10标签构成的氨基酸序列的氨基酸序列所构成的蛋白质的基因。
作为表达载体，可以使用能够由DNA序列表达蛋白质的质粒、噬菌体、病毒等。作为质粒型表达载体，只要能够在宿主细胞内表达目的基因、且其自身能够扩增即可，没有特别限定。例如在使用大肠杆菌Rosetta(DE3)作为宿主的情况下，可以使用pET22b(+)质粒载体、pCold质粒载体等。其中，从蛋白质的生产率的观点出发，优选使用pET22b(+)质粒载体。作为宿主，可以使用例如动物细胞、植物细胞、微生物等。
本发明中使用的多肽优选为作为十字园蛛(Araneus diadematus)的两种主要牵引丝蛋白之一的ADF3来源的多肽。该多肽的强伸度和韧性基本较高，还可以列举容易合成作为优点。
实施例
以下，利用实施例进一步详细地对本发明进行说明，但只要不脱离本发明的技术构思，本发明并不受这些实施例的限制。
<基因合成>
(1)ADF3Kai的基因的合成
从NCBI网络数据库获取作为十字园蛛的两种主要牵引丝蛋白之一的ADF3的部分氨基酸序列(NCBI登录号：AAC47010、GI：1263287)，委托GenScript公司合成编码在该序列的N末端附加有由起始密码子、His10标签和HRV3C蛋白酶(人鼻病毒3C蛋白酶)识别位点构成的(序列号4)的氨基酸序列(序列号5)的基因。其结果，获取了导入有由序列号6所示的碱基序列构成的ADF3Kai的基因的pUC57载体(在紧挨基因的5’末端的上游具有NdeI位点，并且在紧挨基因的5’末端的下游具有Xba I位点)。然后，用Nde I和EcoR I对该基因进行限制酶处理，重组至pET22b(+)表达载体中。
(2)ADF3Kai-noNR的基因的合成
以上述中得到的导入有ADF3Kai的基因的pET22b(+)载体作为模板，通过使用PrimeStar MutagenesisBasal试剂盒(宝生物株式会社制造)的定点突变导入，使ADF3Kai的氨基酸序列(序列号5)中的第543位氨基酸残基缬氨酸(Val)所对应的密码子GTG突变为终止密码子TAA，在pET22b(+)上构建序列号11所示的ADF3Kai-noNR的基因。关于突变导入的准确性，通过使用3130xl Genetic Analyzer(Applied Biosystems)的测序反应来确认。需要说明的是，ADF3Kai-noNR的氨基酸序列如序列号7所示。
<蛋白质的表达>
将上述中得到的包含ADF3Kai-noNR的基因序列的pET22b(+)表达载体转化至大肠杆菌Rosetta(DE3)中。将所得到的单菌落在含有氨苄青霉素的2mL的LB培养基中培养15小时后，将该培养液1.4mL添加至含有氨苄青霉素的140mL的LB培养基中，在37℃、200rpm的条件下培养至培养液的OD600达到3.5为止。接着，将OD600为3.5的培养液与50％葡萄糖140mL一同添加至含有氨苄青霉素的7L的2×YT培养基中，进一步培养至OD600达到4.0为止。然后，向所得到的OD600为4.0的培养液中以终浓度达到0.5mM的方式添加异丙基-β-硫代吡喃半乳糖苷(IPTG)，诱导蛋白质表达。在添加IPTG后经过2小时的时刻，将培养液离心分离，回收菌体。使由添加IPTG前和添加IPTG后的培养液制备的蛋白质溶液在聚丙烯酰胺凝胶中进行电泳，结果，依赖于IPTG添加地观察到目标大小的条带，确认到目的蛋白质进行了表达。将表达ADF3Kai-noNR的蛋白质的大肠杆菌在冷冻室(-20℃)中保存。
<多肽制备例>
(I)在离心管(50mL)中添加表达ADF3Kai-noNR的蛋白质的大肠杆菌的菌体约4.5g和缓冲液AI(20mMTris-HCl、pH7.4)30mL，利用混合器(GE公司制造、SI-0286、级别10)使菌体分散后，利用离心分离机(TOMY SEIKO制造、MX-305)进行离心分离(10000rpm、10分钟、室温)，弃去上清。
(II)在通过离心分离得到的沉淀物(菌体)中添加缓冲液AI 30mL和0.1M的PMSF(用异丙醇溶解)0.3mL，利用上述GE公司制造的混合器(级别10)分散3分钟。然后，使用超声波破碎机(SONIC&MATERIALSINC制造、VCX500)将菌体破碎，进行离心分离(10000rpm、10分钟、室温)。
(III)在通过离心分离得到的沉淀物中加入缓冲液AI 30mL，利用混合器(IKA公司制造、T18basic ULTRA-TURRAX、级别2)分散3分钟后，利用上述TOMY SEIKO制造的离心分离机进行离心分离(10000rpm、10分钟、室温)，除去上清。
(IV)在弃去上清后的离心管中加入7.5M的尿素缓冲液I(7.5M尿素、10mM磷酸二氢钠、20mM NaCl、1mM Tris-HCl、pH7.0)，利用上述SMT公司制造的超声波破碎机(级别7)使沉淀充分分散。然后，利用上述TAITEC公司制造的振荡器(200rpm、60℃)溶解120分钟。将溶解后的蛋白质溶液利用上述TOMY SEIKO制造的离心分离机进行离心分离(11000×g、10分钟、室温)，使用透析管(三光纯药株式会社、纤维素管36/32)将上清在水中进行透析。通过离心分离回收透析后得到的白色凝聚蛋白质，利用冷冻干燥机除去水分，回收冷冻干燥粉末。所得到的冷冻干燥粉末中的目的蛋白质ADF3Kai-noNR的纯化度通过使用Totallab(nonlineardynamics ltd.)对粉末的聚丙烯酰胺凝胶电泳(CBB染色)的结果进行图像分析来确认。其结果，ADF3Kai-noNR的纯化度为约85％。
(实施例1)
<模压成形体的制作方法>
量取上述“多肽制备例”中得到的冷冻干燥粉末(以下称为“样品”)1.35g，将该样品导入至图1所示的加压成形机10的模具2(为圆柱形状的模具，具有截面为35mm×15mm的长方形的贯通孔)的贯通孔内。此时，以厚度均等的方式加入样品。导入全部样品后，开始模具2的加热，同时使用手动压力机(NPa系统株式会社制造、NT-100H-V09)，通过将上侧销4和下侧销6向贯通孔内插入来进行样品的加压。此时，样品的加压条件控制为40kN。在样品的温度达到200℃时中止加热，利用点式制冷机(TRUSCO NAKAYAMA株式会社制造、TS-25EP-1)进行冷却，在样品的温度达到50℃时取出，进行去毛刺后，得到35mm×15mm×2mm的长方体形状的模压成形体。
在实施例1中，在样品的温度达到200℃时中止加热，利用点式制冷机进行冷却，在样品的温度达到50℃时取出。即，加热温度(X)为200℃，在达到加热温度后立即开始急冷，因此退火时间(Y)为0分钟。
(实施例2)
除了使加热温度(X)为100℃、并且使退火时间(Y)为30分钟、使加压条件为30kN以外，与实施例1同样地得到模压成形体。
<弯曲弹性模量和弯曲强度测定方法>
对于所得到的模压成形体，在恒温恒湿槽(espec公司制造、LHL-113)中在20℃/65％的条件下静置1天后，进行以下的测定。
即，在AUTOGRAPH(电子万能试验机)(岛津制作所株式会社制造、AG-X plus)中使用笼夹具进行三点弯曲试验。所使用的测力传感器为50kN。此时，将三点弯曲的支点间距离固定为27mm，使测定速度为1mm/分钟。另外，利用千分尺测定模压成形体的尺寸，设置于夹具上进行测定。弯曲弹性模量由直至0.05～0.25％的位移(变形)求出。
<透明性测定方法>
对于所得到的模压成形体，通过目视测定厚度方向(2mm厚)的透明性，将具有透明性的情况作为○，将不具有透明性的情况作为×。即，将模压成形体放置于印刷有Spiber(丝芭博)公司的标志的纸上，通过能否看见标志来确认透明性。
(比较例1～4)
使用聚醚醚酮(PEEK)、聚碳酸酯(PC)、聚甲基丙烯酸甲酯(PMMA)、ABS树脂(ABS)，与实施例1同样地得到35mm×15mm×2mm的长方体形状的成形体。对于这些成形体，在恒温恒湿槽(espec公司制造、LHL-113)中在20℃/65％的条件下静置1天后，与实施例1同样地测定弯曲弹性模量、弯曲强度和透明性。
将实施例和比较例的结果归纳示于下述表1中。将评价实施例1的透明性时的模压成形体的照片示于图3中。
[表1]
(实施例2～17)
如下述表2所示改变加热温度(X)和退火时间(Y)，并使加压条件为30kN，除此以外，与实施例1同样地得到模压成形体。
[表2]
(实施例18～23)
加热温度(X)、退火时间(Y)和加压条件如下述表3所示，除此以外，与实施例1同样地得到模压成形体。
[表3]
对于实施例5～7、16～17，与实施例1同样地测定弯曲弹性模量和弯曲强度，归纳于表4中。
[表4]
标号说明
2…模具、4…上侧销、6…下侧销、8a…加热加压前的组合物、8b…加热加压后的组合物、10…加压成形机。
序列表
<110> 丝芭博株式会社(Spiber Inc.)
小岛冲压工业株式会社(KOJIMA INDUSTRIES CORPORATION)
技术哈马株式会社(TEKUNOHAMA CO., LTD)
国立大学法人室兰工业大学(MURORAN INSTITUTE OF TECHNOLOGY)
<120> 模压成形体和模压成形体的制造方法(MOLDED MATERIAL)
<130> 2015PS003WO1
<160> 11
<170> PatentIn version 3.5
<210> 1
<211> 50
<212> PRT
<213> Araneus diadematus
<400> 1
Ser Gly Cys Asp Val Leu Val Gln Ala Leu Leu Glu Val Val Ser Ala
1 5 10 15
Leu Val Ser Ile Leu Gly Ser Ser Ser Ile Gly Gln Ile Asn Tyr Gly
20 25 30
Ala Ser Ala Gln Tyr Thr Gln Met Val Gly Gln Ser Val Ala Gln Ala
35 40 45
Leu Ala
50
<210> 2
<211> 30
<212> PRT
<213> Araneus diadematus
<400> 2
Ser Gly Cys Asp Val Leu Val Gln Ala Leu Leu Glu Val Val Ser Ala
1 5 10 15
Leu Val Ser Ile Leu Gly Ser Ser Ser Ile Gly Gln Ile Asn
20 25 30
<210> 3
<211> 21
<212> PRT
<213> Araneus diadematus
<400> 3
Ser Gly Cys Asp Val Leu Val Gln Ala Leu Leu Glu Val Val Ser Ala
1 5 10 15
Leu Val Ser Ile Leu
20
<210> 4
<211> 24
<212> PRT
<213> Artificial Sequence
<220>
<223> His tag and start codon
<400> 4
Met His His His His His His His His His His Ser Ser Gly Ser Ser
1 5 10 15
Leu Glu Val Leu Phe Gln Gly Pro
20
<210> 5
<211> 660
<212> PRT
<213> Artificial Sequence
<220>
<223> recombinant spider silk protein ADF3Kai
<400> 5
Met His His His His His His His His His His Ser Ser Gly Ser Ser
1 5 10 15
Leu Glu Val Leu Phe Gln Gly Pro Ala Arg Ala Gly Ser Gly Gln Gln
20 25 30
Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly
35 40 45
Pro Tyr Gly Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly Tyr
50 55 60
Gly Pro Gly Ser Gly Gln Gln Gly Pro Ser Gln Gln Gly Pro Gly Gln
65 70 75 80
Gln Gly Pro Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ala Ser Ala Ala
85 90 95
Ala Ala Ala Ala Gly Gly Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro
100 105 110
Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ser Ser Ala Ala Ala Ala Ala
115 120 125
Ala Gly Gly Asn Gly Pro Gly Ser Gly Gln Gln Gly Ala Gly Gln Gln
130 135 140
Gly Pro Gly Gln Gln Gly Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala
145 150 155 160
Gly Gly Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly
165 170 175
Pro Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ala Ser Ala Ala Ala Ala
180 185 190
Ala Ala Gly Gly Tyr Gly Pro Gly Ser Gly Gln Gly Pro Gly Gln Gln
195 200 205
Gly Pro Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ala Ser Ala Ala Ala
210 215 220
Ala Ala Ala Gly Gly Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro Gly
225 230 235 240
Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly Gln Gly Pro Tyr Gly
245 250 255
Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly Tyr Gly Pro Gly
260 265 270
Tyr Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly Gln Gly Pro
275 280 285
Tyr Gly Pro Gly Ala Ser Ala Ala Ser Ala Ala Ser Gly Gly Tyr Gly
290 295 300
Pro Gly Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly Gln
305 310 315 320
Gly Pro Tyr Gly Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly
325 330 335
Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly
340 345 350
Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly Gln Gly Pro Tyr Gly
355 360 365
Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly Tyr Gly Pro Gly
370 375 380
Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro
385 390 395 400
Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly
405 410 415
Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly
420 425 430
Gln Gly Ala Tyr Gly Pro Gly Ala Ser Ala Ala Ala Gly Ala Ala Gly
435 440 445
Gly Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro
450 455 460
Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly
465 470 475 480
Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Tyr Gly
485 490 495
Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly Tyr Gly Pro Gly
500 505 510
Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro
515 520 525
Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ala Ala Ser Ala Ala Val Ser
530 535 540
Val Gly Gly Tyr Gly Pro Gln Ser Ser Ser Val Pro Val Ala Ser Ala
545 550 555 560
Val Ala Ser Arg Leu Ser Ser Pro Ala Ala Ser Ser Arg Val Ser Ser
565 570 575
Ala Val Ser Ser Leu Val Ser Ser Gly Pro Thr Lys His Ala Ala Leu
580 585 590
Ser Asn Thr Ile Ser Ser Val Val Ser Gln Val Ser Ala Ser Asn Pro
595 600 605
Gly Leu Ser Gly Cys Asp Val Leu Val Gln Ala Leu Leu Glu Val Val
610 615 620
Ser Ala Leu Val Ser Ile Leu Gly Ser Ser Ser Ile Gly Gln Ile Asn
625 630 635 640
Tyr Gly Ala Ser Ala Gln Tyr Thr Gln Met Val Gly Gln Ser Val Ala
645 650 655
Gln Ala Leu Ala
660
<210> 6
<211> 1983
<212> DNA
<213> Artificial Sequence
<220>
<223> recombinant DNA of spider silk protein gene ADF3Kai
<400> 6
atgcatcacc atcatcatca tcaccaccac cattcctcgg gctcatcctt ggaagtgtta 60
tttcaaggac cagcacgagc cggttcggga caacaagggc ctggccagca gggcccaggt 120
caacaagggc caggacagca gggtccttat gggcccggcg caagcgcagc agctgcggcc 180
gctggtggct atggtcctgg ctccggtcaa cagggccctt cgcaacaagg tcccgggcag 240
caaggtcctg gtggccaggg tccctacggg ccgggggcga gtgcggcagc agccgctgca 300
ggcggttatg gtccaggaag cggacagcaa ggtccgggag gtcaaggtcc gtatggccca 360
ggctctagcg cggctgccgc tgccgcgggt ggcaacggac cagggagcgg acaacagggc 420
gcgggacaac agggtccagg acagcaaggc ccaggggcgt cggcggctgc agcggcggcc 480
ggaggctatg gacccggctc aggacaacag ggaccgggtc aacaaggacc cggtggccaa 540
ggcccctatg gcccgggcgc cagcgcggcc gcagccgccg cgggcgggta cggccccggt 600
agcggccagg gaccaggtca gcaggggcca ggaggtcagg gcccatacgg tccgggcgca 660
tccgcggcgg cggcagcggc aggtggctac ggtcccggaa gcggccaaca ggggccaggg 720
caacaaggac caggacaaca aggtcctggg ggccaaggac cgtatggacc aggagcatca 780
gctgcagccg cggcagctgg cggttacggt ccaggctacg gccagcaggg tccgggtcag 840
cagggaccgg gaggccaggg gccttatggc cctggcgctt ccgcagccag tgccgcttct 900
ggaggatacg ggccgggaag cggtcagcaa ggccctggcc aacaaggacc tggaggccaa 960
gggccctacg gcccaggagc ctcggcagcc gcagctgccg caggtgggta tgggccaggt 1020
agcgggcaac aagggccggg tcagcaagga ccggggcaac agggacctgg gcagcaagga 1080
cccgggggtc aaggcccgta cggacctggt gcgtctgcag ctgctgctgc ggctggtgga 1140
tatggtccgg gatcggggca gcagggtccc ggtcagcagg gccctggtca gcaagggcca 1200
ggccaacagg gacccggaca acaaggcccg ggtcaacagg gtcctggaca gcaggggccg 1260
ggccaacaag gccctgggca acagggtccg gggggacagg gggcctatgg gcctggcgca 1320
tctgccgccg ctggcgcagc cggtgggtac gggcctgggt caggtcaaca ggggcctggt 1380
caacaaggcc ccgggcaaca gggccccggc cagcaaggtc cagggcagca gggcccggga 1440
cagcaagggc ctggacaaca ggggcccgga cagcagggac cttacgggcc cggtgcgagc 1500
gcagcggccg ccgccgcagg gggatatggc cccggatcgg gccagcaggg accaggccag 1560
caaggacctg gccaacaggg cccggggggt caggggccgt atggtcccgg cgctgcaagt 1620
gctgcagtgt ccgttggagg ttacggccct cagtcttcgt ctgttccggt ggcgtccgca 1680
gttgcgagta gactgtcttc acctgctgct tcatcgcgag tatcgagcgc tgtttcgtct 1740
cttgtctcgt cgggtcccac gaaacatgcc gccctttcaa atacgatttc atctgtagtg 1800
tcccaagtta gtgcaagtaa cccggggtta tccggatgcg acgttctcgt tcaggcactc 1860
ctagaagtag tatccgcgtt ggtgagcatc ttaggcagct cctcgatagg tcaaataaac 1920
tatggtgctt cagcccagta tacacagatg gtgggacaga gcgtcgcgca ggcattggct 1980
taa 1983
<210> 7
<211> 542
<212> PRT
<213> Artificial Sequence
<220>
<223> recombinant DNA of spider silk protein gene ADF3Kai
<400> 7
Met His His His His His His His His His His Ser Ser Gly Ser Ser
1 5 10 15
Leu Glu Val Leu Phe Gln Gly Pro Ala Arg Ala Gly Ser Gly Gln Gln
20 25 30
Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly
35 40 45
Pro Tyr Gly Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly Tyr
50 55 60
Gly Pro Gly Ser Gly Gln Gln Gly Pro Ser Gln Gln Gly Pro Gly Gln
65 70 75 80
Gln Gly Pro Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ala Ser Ala Ala
85 90 95
Ala Ala Ala Ala Gly Gly Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro
100 105 110
Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ser Ser Ala Ala Ala Ala Ala
115 120 125
Ala Gly Gly Asn Gly Pro Gly Ser Gly Gln Gln Gly Ala Gly Gln Gln
130 135 140
Gly Pro Gly Gln Gln Gly Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala
145 150 155 160
Gly Gly Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly
165 170 175
Pro Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ala Ser Ala Ala Ala Ala
180 185 190
Ala Ala Gly Gly Tyr Gly Pro Gly Ser Gly Gln Gly Pro Gly Gln Gln
195 200 205
Gly Pro Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ala Ser Ala Ala Ala
210 215 220
Ala Ala Ala Gly Gly Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro Gly
225 230 235 240
Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly Gln Gly Pro Tyr Gly
245 250 255
Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly Tyr Gly Pro Gly
260 265 270
Tyr Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly Gln Gly Pro
275 280 285
Tyr Gly Pro Gly Ala Ser Ala Ala Ser Ala Ala Ser Gly Gly Tyr Gly
290 295 300
Pro Gly Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly Gln
305 310 315 320
Gly Pro Tyr Gly Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly
325 330 335
Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly
340 345 350
Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly Gln Gly Pro Tyr Gly
355 360 365
Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly Tyr Gly Pro Gly
370 375 380
Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro
385 390 395 400
Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly
405 410 415
Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gly
420 425 430
Gln Gly Ala Tyr Gly Pro Gly Ala Ser Ala Ala Ala Gly Ala Ala Gly
435 440 445
Gly Tyr Gly Pro Gly Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro
450 455 460
Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly
465 470 475 480
Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Tyr Gly
485 490 495
Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Gly Gly Tyr Gly Pro Gly
500 505 510
Ser Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro Gly Gln Gln Gly Pro
515 520 525
Gly Gly Gln Gly Pro Tyr Gly Pro Gly Ala Ala Ser Ala Ala
530 535 540
<210> 8
<211> 434
<212> PRT
<213> Artificial
<220>
<223> Recombinang spider silk protein ADF4Kai
<400> 8
Met His His His His His His His His His His Ser Ser Gly Ser Ser
1 5 10 15
Leu Glu Val Leu Phe Gln Gly Pro Ala Gly Ser Ser Ala Ala Ala Ala
20 25 30
Ala Ala Ala Ser Gly Ser Gly Gly Tyr Gly Pro Glu Asn Gln Gly Pro
35 40 45
Ser Gly Pro Val Ala Tyr Gly Pro Gly Gly Pro Val Ser Ser Ala Ala
50 55 60
Ala Ala Ala Ala Ala Gly Ser Gly Pro Gly Gly Tyr Gly Pro Glu Asn
65 70 75 80
Gln Gly Pro Ser Gly Pro Gly Gly Tyr Gly Pro Gly Gly Ser Gly Ser
85 90 95
Ser Ala Ala Ala Ala Ala Ala Ala Ala Ser Gly Pro Gly Gly Tyr Gly
100 105 110
Pro Gly Ser Gln Gly Pro Ser Gly Pro Gly Gly Ser Gly Gly Tyr Gly
115 120 125
Pro Gly Ser Gln Gly Ala Ser Gly Pro Gly Gly Pro Gly Ala Ser Ala
130 135 140
Ala Ala Ala Ala Ala Ala Ala Ala Ala Ser Gly Pro Gly Gly Tyr Gly
145 150 155 160
Pro Gly Ser Gln Gly Pro Ser Gly Pro Gly Ala Tyr Gly Pro Gly Gly
165 170 175
Pro Gly Ser Ser Ala Ala Ala Ala Ala Ala Ala Ala Ser Gly Pro Gly
180 185 190
Gly Tyr Gly Pro Gly Ser Gln Gly Pro Ser Gly Pro Gly Val Tyr Gly
195 200 205
Pro Gly Gly Pro Gly Ser Ser Ala Ala Ala Ala Ala Ala Ala Gly Ser
210 215 220
Gly Pro Gly Gly Tyr Gly Pro Glu Asn Gln Gly Pro Ser Gly Pro Gly
225 230 235 240
Gly Tyr Gly Pro Gly Gly Ser Gly Ser Ser Ala Ala Ala Ala Ala Ala
245 250 255
Ala Ala Ser Gly Pro Gly Gly Tyr Gly Pro Gly Ser Gln Gly Pro Ser
260 265 270
Gly Pro Gly Gly Ser Gly Gly Tyr Gly Pro Gly Ser Gln Gly Gly Ser
275 280 285
Gly Pro Gly Ala Ser Ala Ala Ala Ala Ala Ala Ala Ala Ser Gly Pro
290 295 300
Gly Gly Tyr Gly Pro Gly Ser Gln Gly Pro Ser Gly Pro Gly Tyr Gln
305 310 315 320
Gly Pro Ser Gly Pro Gly Ala Tyr Gly Pro Ser Pro Ser Ala Ser Ala
325 330 335
Ser Val Ala Ala Ser Val Tyr Leu Arg Leu Gln Pro Arg Leu Glu Val
340 345 350
Ser Ser Ala Val Ser Ser Leu Val Ser Ser Gly Pro Thr Asn Gly Ala
355 360 365
Ala Val Ser Gly Ala Leu Asn Ser Leu Val Ser Gln Ile Ser Ala Ser
370 375 380
Asn Pro Gly Leu Ser Gly Cys Asp Ala Leu Val Gln Ala Leu Leu Glu
385 390 395 400
Leu Val Ser Ala Leu Val Ala Ile Leu Ser Ser Ala Ser Ile Gly Gln
405 410 415
Val Asn Val Ser Ser Val Ser Gln Ser Thr Gln Met Ile Ser Gln Ala
420 425 430
Leu Ser
<210> 9
<211> 355
<212> PRT
<213> Artificial
<220>
<223> Recombinant spider silk protein MaSp2_N
<400> 9
Met His His His His His His Ser Ser Gly Ser Ser Leu Glu Val Leu
1 5 10 15
Phe Gln Gly Pro Ala Arg Ala Gly Pro Gly Gly Tyr Arg Pro Gly Gln
20 25 30
Gln Gly Pro Ser Gly Pro Gly Ser Ala Ala Ala Ala Ala Ala Ala Ala
35 40 45
Ala Gly Pro Gly Gly Tyr Gly Pro Gly Gln Gln Gly Pro Gly Gly Tyr
50 55 60
Gly Pro Gly Gln Gln Gly Pro Ser Gly Ala Gly Ser Ala Ala Ala Ala
65 70 75 80
Ala Ala Ala Gly Pro Gly Gln Gln Gly Leu Gly Gly Tyr Gly Pro Gly
85 90 95
Gln Gln Gly Pro Gly Gly Tyr Gly Pro Gly Gln Gln Gly Pro Gly Gly
100 105 110
Tyr Gly Pro Gly Ser Ala Ser Ala Ala Ala Ala Ala Ala Gly Pro Gly
115 120 125
Gln Gln Gly Pro Gly Gly Tyr Gly Pro Gly Gln Gln Gly Pro Ser Gly
130 135 140
Pro Gly Ser Ala Ser Ala Ala Ala Ala Ala Ala Gly Pro Gly Gly Tyr
145 150 155 160
Gly Pro Gly Gln Gln Gly Pro Gly Gly Tyr Ala Pro Gly Gln Gln Gly
165 170 175
Pro Ser Gly Pro Gly Ser Ala Ala Ala Ala Ala Ala Ala Ala Arg Ala
180 185 190
Gly Pro Gly Gly Tyr Gly Pro Ala Gln Gln Gly Pro Ser Gly Pro Gly
195 200 205
Ile Ala Ala Ser Ala Ala Ser Ala Gly Pro Gly Gly Tyr Gly Pro Ala
210 215 220
Gln Gln Gly Pro Ala Gly Tyr Gly Pro Gly Ser Ala Val Ala Ala Ser
225 230 235 240
Ala Gly Ala Gly Ser Ala Gly Tyr Gly Pro Gly Ser Gln Ala Ser Ala
245 250 255
Ala Ala Ser Arg Leu Ala Ser Pro Asp Ser Gly Ala Arg Val Ala Ser
260 265 270
Ala Val Ser Asn Leu Val Ser Ser Gly Pro Thr Ser Ser Ala Ala Leu
275 280 285
Ser Ser Val Ile Ser Asn Ala Val Ser Gln Ile Gly Ala Ser Asn Pro
290 295 300
Gly Leu Ser Gly Cys Asp Val Leu Ile Gln Ala Leu Leu Glu Ile Val
305 310 315 320
Ser Ala Cys Val Thr Ile Leu Ser Ser Ser Ser Ile Gly Gln Val Asn
325 330 335
Tyr Gly Ala Ala Ser Gln Phe Ala Gln Val Val Gly Gln Ser Val Leu
340 345 350
Ser Ala Phe
355
<210> 10
<211> 559
<212> PRT
<213> Artificial
<220>
<223> Recombinant spider silk protein Flag_92_short2
<400> 10
Met His His His His His His His His His His Ser Ser Gly Ser Ser
1 5 10 15
Leu Glu Val Leu Phe Gln Gly Pro Gly Ala Gly Gly Ser Gly Pro Gly
20 25 30
Gly Ala Gly Pro Gly Gly Val Gly Pro Gly Gly Ser Gly Pro Gly Gly
35 40 45
Val Gly Pro Gly Gly Ser Gly Pro Gly Gly Val Gly Pro Gly Gly Ser
50 55 60
Gly Pro Gly Gly Val Gly Pro Gly Gly Ala Gly Gly Pro Tyr Gly Pro
65 70 75 80
Gly Gly Ser Gly Pro Gly Gly Ala Gly Gly Ala Gly Gly Pro Gly Gly
85 90 95
Ala Tyr Gly Pro Gly Gly Ser Tyr Gly Pro Gly Gly Ser Gly Gly Pro
100 105 110
Gly Gly Ala Gly Gly Pro Tyr Gly Pro Gly Gly Glu Gly Pro Gly Gly
115 120 125
Ala Gly Gly Pro Tyr Gly Pro Gly Gly Ala Gly Gly Pro Tyr Gly Pro
130 135 140
Gly Gly Ala Gly Gly Pro Tyr Gly Pro Gly Gly Glu Gly Gly Pro Tyr
145 150 155 160
Gly Pro Gly Gly Ser Tyr Gly Pro Gly Gly Ala Gly Gly Pro Tyr Gly
165 170 175
Pro Gly Gly Pro Tyr Gly Pro Gly Gly Glu Gly Pro Gly Gly Ala Gly
180 185 190
Gly Pro Tyr Gly Pro Gly Gly Val Gly Pro Gly Gly Gly Gly Pro Gly
195 200 205
Gly Tyr Gly Pro Gly Gly Ala Gly Pro Gly Gly Tyr Gly Pro Gly Gly
210 215 220
Ser Gly Pro Gly Gly Tyr Gly Pro Gly Gly Ser Gly Pro Gly Gly Tyr
225 230 235 240
Gly Pro Gly Gly Ser Gly Pro Gly Gly Tyr Gly Pro Gly Gly Ser Gly
245 250 255
Pro Gly Gly Tyr Gly Pro Gly Gly Ser Gly Pro Gly Gly Ser Gly Pro
260 265 270
Gly Gly Tyr Gly Pro Gly Gly Ser Gly Pro Gly Gly Ser Gly Pro Gly
275 280 285
Gly Tyr Gly Pro Gly Gly Ser Gly Pro Gly Gly Tyr Gly Pro Gly Gly
290 295 300
Ser Gly Pro Gly Gly Ser Gly Pro Gly Gly Tyr Gly Pro Gly Gly Ser
305 310 315 320
Gly Pro Gly Gly Ser Gly Pro Gly Gly Tyr Gly Pro Gly Gly Ser Gly
325 330 335
Pro Gly Gly Phe Gly Pro Gly Gly Phe Gly Pro Gly Gly Ser Gly Pro
340 345 350
Gly Gly Tyr Gly Pro Gly Gly Ser Gly Pro Gly Gly Ala Gly Pro Gly
355 360 365
Gly Val Gly Pro Gly Gly Phe Gly Pro Gly Gly Ala Gly Pro Gly Gly
370 375 380
Ala Gly Pro Gly Gly Ala Gly Pro Gly Gly Ala Gly Pro Gly Gly Ala
385 390 395 400
Gly Pro Gly Gly Ala Gly Pro Gly Gly Ala Gly Pro Gly Gly Ala Gly
405 410 415
Pro Gly Gly Ala Gly Gly Ala Gly Gly Ala Gly Gly Ala Gly Gly Ser
420 425 430
Gly Gly Ala Gly Gly Ser Gly Gly Thr Thr Ile Ile Glu Asp Leu Asp
435 440 445
Ile Thr Ile Asp Gly Ala Asp Gly Pro Ile Thr Ile Ser Glu Glu Leu
450 455 460
Thr Ile Ser Ala Tyr Tyr Pro Ser Ser Arg Val Pro Asp Met Val Asn
465 470 475 480
Gly Ile Met Ser Ala Met Gln Gly Ser Gly Phe Asn Tyr Gln Met Phe
485 490 495
Gly Asn Met Leu Ser Gln Tyr Ser Ser Gly Ser Gly Thr Cys Asn Pro
500 505 510
Asn Asn Val Asn Val Leu Met Asp Ala Leu Leu Ala Ala Leu His Cys
515 520 525
Leu Ser Asn His Gly Ser Ser Ser Phe Ala Pro Ser Pro Thr Pro Ala
530 535 540
Ala Met Ser Ala Tyr Ser Asn Ser Val Gly Arg Met Phe Ala Tyr
545 550 555
<210> 11
<211> 1629
<212> DNA
<213> Artificial Sequence
<220>
<223> recombinant spider silk protein gene ADF3Kai-noNR
<400> 11
atgcatcacc atcatcatca tcaccaccac cattcctcgg gctcatcctt ggaagtgtta 60
tttcaaggac cagcacgagc cggttcggga caacaagggc ctggccagca gggcccaggt 120
caacaagggc caggacagca gggtccttat gggcccggcg caagcgcagc agctgcggcc 180
gctggtggct atggtcctgg ctccggtcaa cagggccctt cgcaacaagg tcccgggcag 240
caaggtcctg gtggccaggg tccctacggg ccgggggcga gtgcggcagc agccgctgca 300
ggcggttatg gtccaggaag cggacagcaa ggtccgggag gtcaaggtcc gtatggccca 360
ggctctagcg cggctgccgc tgccgcgggt ggcaacggac cagggagcgg acaacagggc 420
gcgggacaac agggtccagg acagcaaggc ccaggggcgt cggcggctgc agcggcggcc 480
ggaggctatg gacccggctc aggacaacag ggaccgggtc aacaaggacc cggtggccaa 540
ggcccctatg gcccgggcgc cagcgcggcc gcagccgccg cgggcgggta cggccccggt 600
agcggccagg gaccaggtca gcaggggcca ggaggtcagg gcccatacgg tccgggcgca 660
tccgcggcgg cggcagcggc aggtggctac ggtcccggaa gcggccaaca ggggccaggg 720
caacaaggac caggacaaca aggtcctggg ggccaaggac cgtatggacc aggagcatca 780
gctgcagccg cggcagctgg cggttacggt ccaggctacg gccagcaggg tccgggtcag 840
cagggaccgg gaggccaggg gccttatggc cctggcgctt ccgcagccag tgccgcttct 900
ggaggatacg ggccgggaag cggtcagcaa ggccctggcc aacaaggacc tggaggccaa 960
gggccctacg gcccaggagc ctcggcagcc gcagctgccg caggtgggta tgggccaggt 1020
agcgggcaac aagggccggg tcagcaagga ccggggcaac agggacctgg gcagcaagga 1080
cccgggggtc aaggcccgta cggacctggt gcgtctgcag ctgctgctgc ggctggtgga 1140
tatggtccgg gatcggggca gcagggtccc ggtcagcagg gccctggtca gcaagggcca 1200
ggccaacagg gacccggaca acaaggcccg ggtcaacagg gtcctggaca gcaggggccg 1260
ggccaacaag gccctgggca acagggtccg gggggacagg gggcctatgg gcctggcgca 1320
tctgccgccg ctggcgcagc cggtgggtac gggcctgggt caggtcaaca ggggcctggt 1380
caacaaggcc ccgggcaaca gggccccggc cagcaaggtc cagggcagca gggcccggga 1440
cagcaagggc ctggacaaca ggggcccgga cagcagggac cttacgggcc cggtgcgagc 1500
gcagcggccg ccgccgcagg gggatatggc cccggatcgg gccagcaggg accaggccag 1560
caaggacctg gccaacaggg cccggggggt caggggccgt atggtcccgg cgctgcaagt 1620
gctgcataa 1629
Claims (3)
1.一种模压成形体，其为包含多肽的组合物的模压成形体，所述多肽为选自由天然蛛丝蛋白和来源于天然蛛丝蛋白的多肽组成的组中的至少一种，所述模压成形体为弯曲弹性模量大于4.5GPa的成形体，所述多肽为下述式(1)所示的多肽，
REP1-REP2(1)
式中，REP1为2～20个丙氨酸连续排列的序列，REP2为由10～200个氨基酸残基构成的氨基酸序列，该氨基酸序列中所含的甘氨酸、丝氨酸、谷氨酰胺和丙氨酸的合计残基数相对于全部氨基酸残基数为40％以上。
2.如权利要求1所述的模压成形体，其中，所述模压成形体为加热加压成形体。
3.一种模压成形体的制造方法，其具备对包含选自由天然蛛丝蛋白和来源于天然蛛丝蛋白的多肽组成的组中的至少一种的多肽的组合物在80～300℃、10kN以上的条件下进行加热和加压的工序，所述多肽为下述式(1)所示的多肽，
REP1-REP2(1)
式中，REP1为2～20个丙氨酸连续排列的序列，REP2为由10～200个氨基酸残基构成的氨基酸序列，该氨基酸序列中所含的甘氨酸、丝氨酸、谷氨酰胺和丙氨酸的合计残基数相对于全部氨基酸残基数为40％以上。
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| JP2015185777 | 2015-09-18 | ||
| JP2015-185777 | 2015-09-18 | ||
| PCT/JP2016/076501 WO2017047504A1 (ja) | 2015-09-18 | 2016-09-08 | モールド成形体及びモールド成形体の製造方法 |
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| CN108137814A CN108137814A (zh) | 2018-06-08 |
| CN108137814B true CN108137814B (zh) | 2021-08-24 |
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| US (1) | US10961285B2 (zh) |
| EP (1) | EP3351584B1 (zh) |
| JP (1) | JP6830604B2 (zh) |
| CN (1) | CN108137814B (zh) |
| WO (1) | WO2017047504A1 (zh) |
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| JP2018159137A (ja) | 2015-08-20 | 2018-10-11 | 国立研究開発法人理化学研究所 | クモ糸様構造を有するポリペプチド繊維の製造方法 |
| JP6551789B2 (ja) * | 2015-12-17 | 2019-07-31 | 国立大学法人室蘭工業大学 | 動物繊維成形物及びその製造方法 |
| EP3502169B1 (en) * | 2016-08-19 | 2021-08-25 | Riken | Composite molding composition including fibroin-like protein, and method for producing composite molding composition |
| US20190194403A1 (en) * | 2016-09-02 | 2019-06-27 | Spiber Inc. | Molded Article and Method for Producing Molded Article |
| JP2020105231A (ja) * | 2017-03-22 | 2020-07-09 | Ｓｐｉｂｅｒ株式会社 | モールド成形体及びモールド成形体の製造方法 |
| JPWO2019054503A1 (ja) * | 2017-09-15 | 2021-01-28 | Ｓｐｉｂｅｒ株式会社 | モールド成形用組成物、成形体及び成形体の製造方法 |
| WO2019117296A1 (ja) * | 2017-12-15 | 2019-06-20 | 国立大学法人室蘭工業大学 | 成形体の製造方法および成形体 |
| JP2021063143A (ja) * | 2017-12-27 | 2021-04-22 | Ｓｐｉｂｅｒ株式会社 | モールド成形体及びモールド成形体の製造方法 |
| CN112135881A (zh) | 2018-04-03 | 2020-12-25 | 丝芭博株式会社 | 成形体及其制造方法 |
| CN109265913A (zh) * | 2018-08-09 | 2019-01-25 | 南京欧纳壹有机光电有限公司 | 一种高强度工程塑料及其制备工艺 |
| JP2020055916A (ja) * | 2018-09-28 | 2020-04-09 | Ｓｐｉｂｅｒ株式会社 | モールド成形体、モールド成形体の製造方法、およびモールド成形体の柔軟性調整方法 |
| JP2021008414A (ja) * | 2019-06-28 | 2021-01-28 | Ｓｐｉｂｅｒ株式会社 | タンパク質層接合体 |
| WO2021066049A1 (ja) | 2019-09-30 | 2021-04-08 | Ｓｐｉｂｅｒ株式会社 | タンパク質接着剤、接合体及びその製造方法 |
| WO2024137617A2 (en) * | 2022-12-19 | 2024-06-27 | Trustees Of Tufts College | Processing and fabrication of composite silk-based plastics |
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| "Effect of preparation method of powdered silk on the mechanical properties of moulded silk";Daijirou Akiyama等;《polymer》;20030422;第35卷(第11期);第2355-2358页 * |
| "Silk Properties Determined by Gland-Specific Expression of a Spider Fibroin Gene Family";Paul A. Guerette等;《Science》;19960405;第272卷(第5258期);第112-115页 * |
| "粉末蚕丝的压制及其模压物的性能";杨如馨;《现代丝绸科学与技术》;19940215(第1期);第8-12页 * |
Also Published As
| Publication number | Publication date |
|---|---|
| EP3351584A1 (en) | 2018-07-25 |
| CN108137814A (zh) | 2018-06-08 |
| WO2017047504A1 (ja) | 2017-03-23 |
| US20190040109A1 (en) | 2019-02-07 |
| EP3351584A4 (en) | 2019-02-06 |
| US10961285B2 (en) | 2021-03-30 |
| JPWO2017047504A1 (ja) | 2018-07-05 |
| JP6830604B2 (ja) | 2021-02-17 |
| EP3351584B1 (en) | 2021-04-07 |
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