化学
组合化学
催化作用
超分子化学
编码
基质(水族馆)
计算生物学
功能(生物学)
底物特异性
纳米技术
分子识别
灵活性(工程)
酶
生物化学
有机化学
分子
遗传学
基因
生物
统计
海洋学
地质学
材料科学
数学
作者
Sara Carvalho,David Q. Peralta Reis,Sara V. Pereira,Daniela Kalafatović,Ana Sofia Pina
标识
DOI:10.1002/ijch.202200029
摘要
Abstract Enzymes’ machinery has been an inspiration for chemists. Peptides are vital players in the origin of life, being ancestors of complex enzymes. Even short peptides that are simple in terms of the number of residues are reprogrammable and built to encode chemical information for catalysis, substrate recognition, and molecular interactions. The combinatorial search of the sequence space led to identifying peptides with catalytic activities. However, most of these sequences remain unevolved, leading to modest rates in aqueous media. Short peptides present conformational flexibility, which is their primary liability for catalysis. To overcome this, supramolecular motifs and secondary frameworks are used as scaffolds to incorporate catalytic residues and improve their efficiency. This review discusses the strategies used to discover and evolve catalytic function in short peptides beyond the de novo design and the advantages of using these approaches to enhance catalysis.
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