Combining flagelliform and dragline spider silk motifs to produce tunable synthetic biopolymer fibers.
Combining flagelliform and dragline spider silk motifs to produce tunable synthetic biopolymer fibers.
复制标题
DOI：
10.1002/bip.21724
复制
发表时间：
2012-06
期刊：
影响因子：
2.9
通讯作者：
Lewis, Randolph V.
中科院分区：
文献类型：
--
作者：
Teule, Florence;Addison, Bennett;Cooper, Alyssa R.;Ayon, Joel;Henning, Robert W.;Benmore, Chris J.;Holland, Gregory P.;Yarger, Jeffery L.;Lewis, Randolph V.
关键词：
重组产生的两种Flag/MaSp 2丝蛋白基于来自棒足环织蜘蛛的拖丝蛛丝蛋白2（MaSp 2）的基本共有重复序列。然而，与聚丙氨酸片段并列的含脯氨酸的五肽类似于在组成网螺旋的鞭毛状丝蛋白（Flag）中发现的那些：（GPGGX 1 GPGGX 2）2，其中X1/X2=A/A或Y/S。当Flag基序为（GPGGX 1-GPGGX 2）2（X1/X2 = Y/S或A/A）时，在水溶液中由蛋白质膜形成纤维或在有机条件下由再溶解的蛋白质原液挤出形成纤维。后纤维加工涉及水处理之前或之后的类似拉伸比（2-2.5×）。将纤维中的结构（ssNMR和XRD）和形态（SEM）变化与每个步骤中纤维的机械性能进行比较。NMR表明，在挤出时形成的聚丙氨酸区域中的β-折叠纳米晶体的分数，在拉伸期间增加，并且在水处理后最大化。X射线衍射表明，平行于纤维轴的纳米晶取向增加了纤维的极限强度和初始刚度。水在塑化无定形区的同时进一步促进了纤维的取向和三维生长，从而由于增加的延展性而产生更坚韧的纤维。这些纤维是高度吸湿的，并且具有相似的内部网络组织，因此取决于它们的直径的机械性能的范围相似。丝样蛋白的共有重复序列的整体结构决定了纤维的机械性能，而蛋白质分子量限制了这些相同的性能。微妙的结构基序重新设计影响蛋白质自组装机制和纤维形成的要求。
The two Flag/MaSp 2 silk proteins produced recombinantly were based on the basic consensus repeat of the dragline silk spidroin 2 protein (MaSp 2) from the Nephila clavipes orb weaving spider. However, the proline-containing pentaptides juxtaposed to the polyalanine segments resembled those found in the flagelliform silk protein (Flag) composing the web spiral: (GPGGX1 GPGGX2)2 with X1/X2=A/A or Y/S. Fibers were formed from protein films in aqueous solutions or extruded from resolubilized protein dopes in organic conditions when the Flag motif was (GPGGX1 GPGGX2)2 with X1/X2 = Y/S or A/A, respectively. Post fiber processing involved similar drawing ratios (2–2.5×) before or after water-treatment. Structural (ssNMR and XRD) and morphological (SEM) changes in the fibers were compared to the mechanical properties of the fibers at each step. NMR indicated that the fraction of β-sheet nanocrystals in the polyalanine regions formed upon extrusion, increased during stretching, and was maximized after water-treatment. XRD showed that nanocrystallite orientation parallel to the fiber axis increased the ultimate strength and initial stiffness of the fibers. Water furthered nanocrystal orientation and three-dimensional growth while plasticizing the amorphous regions, thus producing tougher fibers due to increased extensibility. These fibers were highly hygroscopic and had similar internal network organization, thus similar range of mechanical properties that depended on their diameters. The overall structure of the consensus repeat of the silk-like protein dictated the mechanical properties of the fibers while protein molecular weight limited these same properties. Subtle structural motif redesign impacted protein self-assembly mechanisms and requirements for fiber formation.
登录
查看更多内容
DOI：
10.1039/b812928b
发表时间：
2008-11-21
期刊：
Chemical communications (Cambridge, England)
影响因子：
--
作者：
Holland GP;Jenkins JE;Creager MS;Lewis RV;Yarger JL
通讯作者：
Yarger JL
影响因子：
4.4
作者：
BENNETT, AE;RIENSTRA, CM;GRIFFIN, RG
通讯作者：
GRIFFIN, RG
影响因子：
56.9
作者：
Guerette, PA;Ginzinger, DG;Gosline, JM
通讯作者：
Gosline, JM
影响因子：
3
作者：
Heim, Markus;Ackerschott, Christian B.;Scheibel, Thomas
通讯作者：
Scheibel, Thomas
影响因子：
5.5
作者：
Elices, M.;Guinea, G. V.;Perez-Rigueiro, J.
通讯作者：
Perez-Rigueiro, J.