Catalytic Behavior of Histidine-bearing Self-assembling Peptide for Ester Hydrolysis

Artificial enzyme mimics have lately sparked a lot of attention since they offer a lot of benefits over natural enzymes. Because of their proteic origin and tailorable structures, self-assembling peptides are ideal building blocks for the creation of artificial enzymes. Recently, a series of histidinebearing self-assembling peptides with β-sheet structures, which are selective for short-chain fatty acids, were described. In this work, the catalytic behaviors of these peptides were further investigated using 2,4-dinitrophenyl acetate (DNPA) as a model substrate. Furthermore, the peptide was capable of forming a solid hydrogel that was also catalytically active at higher concentrations.