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.