Extensible collagen in mussel byssus: A natural block copolymer
Extensible collagen in mussel byssus: A natural block copolymer
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DOI：
10.1126/science.277.5333.1830
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发表时间：
1997-09-19
期刊：
影响因子：
56.9
通讯作者：
Waite, JH
中科院分区：
文献类型：
--
作者：
Coyne, KJ;Qin, XX;Waite, JH
为了附着在固体表面，海洋贻贝会产生一根粗线，每根线的一端是坚硬的系绳，另一端是具有160%延伸性的减震器。近端骨节的弹性延伸性是非同寻常的，因为它的结构是胶原蛋白，而且大多数胶原材料的延伸度有限(不到10%)。根据互补DNA，我们推测，在可伸展的近端部分占主导地位的胶原蛋白(PreCol-P)的一级结构编码了一种前所未有的天然嵌段共聚物，具有三种主要结构域类型：中心胶原域、侧翼弹性域和富含组氨酸的终端域。弹性结构域具有与弹性蛋白和蜘蛛丝素蛋白富含甘氨酸的无定形区域非常相似的序列基序。Pre-Col-P的弹性域可赋予双螺纹线延伸性。
To adhere to solid surfaces, marine mussels produce byssal threads, each of which is a stiff tether at one end and a shock absorber with 160 percent extensibility at the other end. The elastic extensibility of proximal byssus is extraordinary given its construction of collagen and the limited extension (less than 10 percent) of most collagenous materials. From the complementary DNA, we deduced that the primary structure of a collagenous protein (preCol-P) predominating in the extensible proximal portion of the threads encodes an unprecedented natural block copolymer with three major domain types: a central collagen domain, flanking elastic domains, and histidine-rich terminal domains. The elastic domains have sequence motifs that strongly resemble those of elastin and the amorphous glycine-rich regions of spider silk fibroins. Byssal thread extensibility may be imparted by the elastic domains of preCol-P.