Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-like properties
Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-like properties
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DOI：
10.1002/bip.10512
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发表时间：
2003-12-01
期刊：
影响因子：
2.9
通讯作者：
Keeley, FW
中科院分区：
文献类型：
--
作者：
Bellingham, CM;Lillie, MA;Keeley, FW
涉及将单体单元自组装成有组织的聚合物阵列的过程是当前备受关注的主题，特别是在纳米技术和生物材料领域。具有自组织潜力的蛋白质聚合物的一个生物学例子是弹性蛋白。弹性蛋白是细胞外基质蛋白质，其赋予大动脉、肺实质和其它组织延展性和弹性回缩性。弹性蛋白原是一种分子量约为70 kDa的可溶性弹性蛋白单体，具有高度非极性的特性，主要由34个疏水和交联结构域组成。交联结构域含有赖氨酸残基，其注定形成稳定聚合物的共价分子间交联。我们和其他人已经提出，疏水结构域是相互作用的网站，有助于并列的赖氨酸残基在交联形成的准备。在这里，使用基于人弹性蛋白序列的重组多肽，我们证明，少至三个疏水结构域侧翼两个交联结构域足以支持自组装过程，对齐赖氨酸的零长度交联，导致天然弹性蛋白的交联的形成。该过程允许制造具有与天然弹性蛋白相似的溶解度和机械性质的聚合物基质。(C)2003 Wiley Periodicals，Inc.
Processes involving self-assembly of monomeric units into organized polymeric arrays are currently the subject of much attention, particularly in the areas of nanotechnology and biomaterials. One biological example of a protein polymer with potential for self-organization is elastin. Elastin is the extracellular matrix protein that imparts the properties of extensibility and elastic recoil to large arteries, lung parenchyma, and other tissues. Tropoelastin, the approximate to70 kDa soluble monomeric form of elastin, is highly nonpolar in character, consisting essentially of 34 alternating hydrophobic and crosslinking domains. Crosslinking domains contain the lysine residues destined to form the covalent intermolecular crosslinks that stabilize the polymer. We and others have suggested that the hydrophobic domains are sites of interactions that contribute to juxtaposition of lysine residues in preparation for crosslink formation. Here, using recombinant polypeptides based on sequences in human elastin, we demonstrate that as few as three hydrophobic domains flanking two crosslinking domains are sufficient to support a self-assembly process that aligns lysines for zero-length crosslinking, resulting in formation of the crosslinks of native elastin. This process allows fabrication of a polymeric matrix with solubility and mechanical properties similar to those of native elastin. (C) 2003 Wiley Periodicals, Inc.