从贻贝胡须中提取肌肉:研究和应用。

L M Rzepecki, J H Waite
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引用次数: 0

摘要

海洋贻贝和斑马贻贝分泌出硬须,以便机会地附着在环境中的坚硬表面上。通过这样做,它们自然赢得了污染害虫的声誉。研究贻贝中足丝蛋白的前体不仅希望找到对付这些海洋污染物的具体措施,而且希望对水下工程粘合剂的技术挑战有一些深入的了解。尽管大纤维蛋白都是将它们粘在表面上的须状胶的一部分,但根据它们在大纤维线中的功能,它们可以被细分为三种类型:(1)纤维蛋白在线的核心形成承重电缆,(2)角质层蛋白在电缆周围形成保护层,(3)粘附蛋白将电缆连接到外部表面。其中任何一个缺陷都会破坏贻贝的附着能力。纤维蛋白可以是胶原蛋白、丝状蛋白、弹性蛋白或这些蛋白的任何组合。表皮蛋白具有表面偶联特性、串联重复的一级序列、高含量的赖氨酸和外来氨基酸3,4-二羟基苯基- l-丙氨酸(DOPA)。黏附蛋白是低分子量的,含有多巴,并组装形成微细胞固体(泡沫)。其中一些蛋白质作为细胞和组织附着因子、防腐蚀剂和金属隔离试剂已经引起了生物技术的关注。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Wresting the muscle from mussel beards: research and applications.

Marine and zebra mussels secrete byssal beards to attach themselves opportunistically to hard surfaces in their environment. By doing this, they naturally earn a reputation as fouling pests. The protein precursors of byssus in mussels are being investigated in the hope not only of discovering specific measures against these marine foulers, but also to gain some insights into the technically challenging task of engineering adhesive bonds underwater. Although byssal proteins are all part of the bearded glue that bonds them to a surface, they can be subdivided into three types depending on the function that they serve in byssal threads: (1) fibrous proteins form the load-bearing cables in the core of the threads, (2) cuticular proteins form a protective coat around the cables, and (3) adhesive proteins connect the cables to a foreign surface. A flaw in any one of these will undermine a mussel's ability to attach. The fibrous proteins can be collagenous, silk-like, elastic, or any combination of these. Covering these are the cuticular proteins, which are distinguished by their surface coupling properties, tandemly repeated primary sequence, and their high content of lysine and the exotic amino acid 3,4-dihydroxyphenyl-L-alanine (DOPA). The adhesive proteins are of low molecular weight, contain DOPA, and assemble to form microcellular solids (foams). Several of these proteins are already attracting biotechnological attention as cell and tissue attachment factors, anticorrosives, and metal-sequestering reagents.

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