Inter-and intramolecular adhesion mechanisms of mussel foot proteins  

作　　者：KAN YaJing WEI ZhiYong TAN QiYan CHEN YunFei 

机构地区：[1]Jiangsu Key Laboratory for Design and Manugacture of Micro-Nano Biomedical Iastruments,and School of Mchanical Enginering.Southeast University,Nanjing 211189,China [2]School of Mechanical Engineering,Nanjing Institute of Technology,Nanjing 211167,China

出　　处：《Science China(Technological Sciences)》2020年第9期1675-1698,共24页中国科学（技术科学英文版）

基　　金：supported by the National Natural Science Foundation of China (Grant No. 51605090);the Natural Science Foundation of Jiangsu Province (Grant Nos. BK20160670 and BK20160776);the Fundamental Research Funds for the Central Universities (Grant No.2242019k1G011)。

摘　　要：Mussel foot proteins(Mfps) secreted in the byssal plaque of marine mussels are widely researched for their relevance to mussel adhesion in water. As the abundant residue in the amino acid sequences of major adhesive proteins, 3,4-dihydroxyphenylalanine(Dopa) or its catecholic moiety plays a key role in both Mfp binding to surface and cohesive cross-linking of Mfps in byssal plaques. The binding performance of an Mfp significantly depends on the content and redox state of Dopa, whereas the types of interaction vary in line with different surface chemistries and p H conditions. Thorough understanding of mussel adhesion from a molecular perspective is crucial to promote the application of synthetic mussel-bionic adhesives. This article presents a brief review of the research progress on the adhesion mechanisms of Mfps, which further emphasizes the contributions of Dopamediated interactions and considers other amino acids and factors. The involved inter-and intramolecular interactions are responsible for not only the diverse adhesion capacities of an adhesive byssal plaque as mussel's adhesion precursor but also the formation and properties of the plaque structure.

关 键 词：mussel foot protein adhesion mechanism DOPA CATECHOL surface forces apparatus 

分 类 号：TB391[一般工业技术—材料科学与工程]