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

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

Volume: 20 Issue: 10

Author(s): Yanfei Liu*, Lei Huang, Peili Feng, Luoying Chen, Huanhuan He and Hui Chen

Affiliation:

• Key Laboratory of Cell Engineering of Guizhou Province, Affiliated Hospital of Zunyi Medical University, Zunyi, China
• The Clinical Stem Cell Research Institute, Affiliated Hospital of Zunyi Medical University, Zunyi, China
• Collaborative Innovation Center of Chinese Ministry of Education, Zunyi Medical University, Zunyi, China

Abstract: 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.

Cite this article as:

Liu Yanfei*, Huang Lei, Feng Peili, Chen Luoying, He Huanhuan and Chen Hui, Catalytic Behavior of Histidine-bearing Self-assembling Peptide for Ester Hydrolysis, Letters in Organic Chemistry 2023; 20 (10) . https://dx.doi.org/10.2174/1570178620666230428111754