Enzyme-Directed Functionalization of Designed, Two-Dimensional Protein Lattices.

ABSTRACT: The design and construction of crystalline protein arrays to selectively assemble ordered nanoscale materials have potential applications in sensing, catalysis, and medicine. Whereas numerous designs have been implemented for the bottom-up construction of protein assemblies, the generation of artificial functional materials has been relatively unexplored. Enzyme-directed post-translational modifications are responsible for the functional diversity of the proteome and, thus, could be harnessed to selectively modify artificial protein assemblies. In this study, we describe the use of phosphopantetheinyl transferases (PPTases), a class of enzymes that covalently modify proteins using coenzyme A (CoA), to site-selectively tailor the surface of designed, two-dimensional (2D) protein crystals. W

SUBMITTER: Subramanian RH 

PROVIDER: S-EPMC7855359 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature