(391e) Enzyme-Reactive Self-Assembling Peptides for Biomacromolecular Functionalization
Herein we developed novel peptide assemblies that can be further functionalized with biomacromolecules using enzyme catalysis. The enzyme used in our study is microbial transglutaminase, MTG. MTG catalyzes the acyl transfer reaction between Î³-carboxyamide of glutamine (Q) residues and Îµ-amino group of lysine (K) residues or primary amines. MTG-recognizable self-assembling peptides were designed by introducing aromatic group and hydrophobic amino acid sequence at the N-terminal of Q. As a biomacromolecule, enhanced green fluorescent protein (EGFP) was employed, of which C-terminal was attached with the MTG-recognizable lysine-containing sequence, K-tag. We synthesized several self-assembling peptides and investigated the influence of the assembled structures on the MTG reactivity. The enzymatic functionalization of EGFP on the peptides structures was also examined.