Elastin as a self-organizing biomaterial: use of recombinantly expressed human elastin polypeptides as a model for investigations of structure and self-assembly of elastin
Elastin as a self-organizing biomaterial: use of recombinantly expressed human elastin polypeptides as a model for investigations of structure and self-assembly of elastin
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DOI：
10.1098/rstb.2001.1027
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发表时间：
2002-02-28
影响因子：
6.3
通讯作者：
Woodhouse, KA
中科院分区：
文献类型：
--
作者：
Keeley, FW;Bellingham, CM;Woodhouse, KA
弹性蛋白是大动脉如主动脉的主要细胞外基质蛋白，赋予延展性和弹性回缩的特性。一旦被放置在组织中，聚合弹性蛋白就不受周转的影响，而是能够通过数千万次的伸展和回缩循环来维持其机械弹性。弹性蛋白由Ca.具有交替的疏水和交联特性的36个结构域。已经表明，这些疏水结构域主要含有甘氨酸、脯氨酸、亮氨酸和缬氨酸，通常以串联重复序列存在，负责弹性蛋白对齐单体链以进行共价交联的能力。我们已经表明，基于人弹性蛋白序列的重组表达的小多肽含有足够的信息来自组织成纤维状结构并促进赖氨酸衍生的交联的形成。这些交联的多肽也可以被制造成具有使人联想到天然不溶性弹性蛋白的溶解度和机械性质的膜结构。了解弹性蛋白多肽自组织能力的基础可能为自组装生物材料的一般设计提供重要线索。
Elastin is the major extracellular matrix protein of large arteries such as the aorta, imparting characteristics of extensibility and elastic recoil. Once laid down in tissues, polymeric elastin is not subject to turnover, but is able to sustain its mechanical resilience through thousands of millions of cycles of extension and recoil. Elastin consists of ca. 36 domains with alternating hydrophobic and cross-linking characteristics. It has been suggested that these hydrophobic domains, predominantly containing glycine, proline, leucine and valine, often occurring in tandemly repeated sequences, are responsible for the ability of elastin to align monomeric chains for covalent cross-linking. We have shown that small, recombinantly expressed polypeptides based on sequences of human elastin contain sufficient information to self-organize into fibrillar structures and promote the formation of lysine-derived cross-links. These cross-linked polypeptides can also be fabricated into membrane structures that have solubility and mechanical properties reminiscent of native insoluble elastin. Understanding the basis of the self-organizational ability of elastin-based polypeptides may provide important clues for the general design of self-assembling biomaterials.