Nonfouling Coatings from Synthetic Intrinsically Disordered Proteins.

ABSTRACT: The antifouling performance of a previously developed triblock protein, B-M-E is optimized, that self-assembles on gold surfaces to form a nonfouling layer by modifying the sequence of its E block. In this protein, B is a gold-binding domain, M is a trimerization domain, and E is a synthetic intrinsically disordered protein (IDP) that confers nonfouling behavior. To identify optimal sequences for the nonfouling E block, a few candidate IDPs are screened that provide a proxy for nonfouling behavior, such as extending the half-life of their fusion partners in systemic circulation and sequences that promote soluble expression of their fusion partners in E coli. One IDP is identified with the sequence [(GAGAIP)₃-(GAGEIP)]₄ as the E block in B-M-E brush on gold, forming a

SUBMITTER: Zheng C 

PROVIDER: S-EPMC12393014 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature