Enzymatic Halogenation of Silk Fibroin from.

ABSTRACT: Silk fibroin from the silkworm, , is a unique biomaterial that has been extensively studied for a variety of applications that utilize robust mechanical properties, biological compatibility, and controlled self-assembly properties. This study tested carbon-halogen (C-X) bond halogenation to alter the chemical composition of silk fibroin with the intention to generate novel functional materials. In brief, silk fibroin side-chain modification used halogen salts (NaX, X = Cl, Br, and I), hydrogen peroxide (H₂O₂), and the vanadium-dependent haloperoxidase from to produce primarily halogenated tyrosine residues along the amorphous regions of the silk fibroin protein. Halogenation was confirmed with various methods, including 1D ¹H NMR, X-ray photoelectron spectr

SUBMITTER: Mancini JA 

PROVIDER: S-EPMC12311704 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature