Peptides and peptidomimetics as inhibitors of protein-protein interactions involving β-sheet secondary structures

被引:36
|
作者
Arenas, Jose Laxio [1 ]
Kaffy, Julia [1 ]
Ongeri, Sandrine [1 ]
机构
[1] Univ Paris Saclay, Univ Paris Sud, BioCIS, CNRS, 5 Rue Jean Baptiste Clement, F-92296 Chatenay Malabry, France
关键词
ISLET AMYLOID POLYPEPTIDE; RAS-EFFECTOR INTERACTIONS; FIBRIL FORMATION; MOLECULAR TONGS; HAIRPIN MIMICS; WILD-TYPE; AGGREGATION; MODULATORS; DIMERIZATION; DESIGN;
D O I
10.1016/j.cbpa.2019.07.008
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein-protein interactions involving beta-sheet secondary structures have been questioned in many fatal human diseases such as cancer, autoimmune and neurodegenerative diseases. Small selective peptide derivatives and analogues are promising drug candidates for inhibiting this poorly known class of PPIs. In this review, we will highlight the main strategies developed for designing linear and cyclic peptide and peptidomimetic inhibitors of PPIs involving beta-sheet structures. These compounds either do not adopt preferred conformations or can mimic protein secondary structures such as beta-strands, beta-hairpins or alpha-helices.
引用
收藏
页码:157 / 167
页数:11
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