Catalytic amyloids

被引:20
|
作者
Arad, Elad [1 ,2 ]
Jelinek, Raz [1 ,2 ]
机构
[1] Ben Gurion Univ Negev, Ilse Katz Inst Nanoscale Sci & Technol, IL-8410501 Beer Sheva, Israel
[2] Ben Gurion Univ Negev, Dept Chem, IL-8410501 Beer Sheva, Israel
来源
TRENDS IN CHEMISTRY | 2022年 / 4卷 / 10期
关键词
ALZHEIMERS-DISEASE; OXIDATIVE STRESS; SERYL-HISTIDINE; BETA PEPTIDE; PROTEIN; HYDROLASE; DESIGN; SCAFFOLD; COPPER; HYDROLYSIS;
D O I
10.1016/j.trechm.2022.07.001
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Protein amyloids generally constitute beta-sheet rich fibrillar assemblies. Amyloid fibrils have been identified in varied diseases, formed by bacterially secreted proteins, and generated in de novo designed peptides. This review article summarizes the burgeoning body of work reporting catalytic properties of amy-loid fibrils. We highlight representative studies focusing on catalytic amyloid peptides, both synthetic and naturally occurring. We discuss the structural features associated with catalysis and putative catalytic sites on amyloid fibrils' surfaces. We also highlight studies demonstrating catalytic functions of short amyloid-like sequences and their possible involvement in early-life reactions, acting as primitive enzymes. Finally, we discuss recent reports of the catalytic activities of native amyloids, pointing to possible roles of amyloid catalysis in disease progression and pathologies.
引用
收藏
页码:907 / 917
页数:11
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