| Literature DB >> 30843382 |
Haishan Qi1, Weiwei Zheng1, Chen Zhang1, Xiao Zhou1, Lei Zhang1,2.
Abstract
Surface functionalization can effectively endow materials with desirable properties, promoting the performance between the material and environment, with extensive applications. However, a universal and straightforward surface functionalization method with biocompatibility is scarce. In this study, with synthetic biology strategy, recombinant mussel plaque protein with a zwitterionic peptide inspired by molecular chaperone was engineered through post-translational modification, in which 3,4-dihydroxyphenylalanine was residue-specifically obtained efficiently from tyrosine with tyrosinase coexpressed in vivo. The rational designed chimeric protein coating in this work could successfully anchor to various substrates and exhibit excellent antifouling performance in resisting protein adsorption, cell attachment, and bacterial adhesion with eminent biocompatibility.Entities:
Keywords: 3,4-dihydroxyphenylalanine; post-translational modification; protein engineering; surface chemistry; universal coating
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Year: 2019 PMID: 30843382 DOI: 10.1021/acsami.8b22551
Source DB: PubMed Journal: ACS Appl Mater Interfaces ISSN: 1944-8244 Impact factor: 9.229