RNA-Binding Peptides Inspired by the RNA Recognition Motif

被引:0
|
作者
Marshall, Luke K. [1 ,2 ]
Fahrenbach, Albert C. [3 ,4 ]
Thordarson, Pall [3 ,4 ]
机构
[1] Univ New South Wales, Sch Chem, Sydney, NSW 2052, Australia
[2] Univ New South Wales, Australian Ctr Astrobiol, Sydney, NSW 2052, Australia
[3] Univ New South Wales, Australian Ctr Astrobiol, Sch Chem, Sydney, NSW 2052, Australia
[4] Univ New South Wales, UNSW RNA Inst, Sydney, NSW 2052, Australia
基金
澳大利亚研究理事会;
关键词
BETA-HAIRPIN PEPTIDE; STRUCTURAL INSIGHTS; MOLECULAR-BASIS; PROTEINS; DESIGN; ORIGIN; EVOLUTION; TRPZIP; SEQUENCE; MIMICS;
D O I
10.1021/acschembio.3c00694
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
beta-Hairpin peptides with RNA-binding sequences mimicking the central two beta-strands of the RNA recognition motif (RRM) protein domain have been observed to bind in a 2:1 fashion to a series of RNA homooligonucleotides in aqueous solution (PBS buffer, pH 7.40) with binding energies (-27 to -35 kJ mol(-1)) similar to those of full-size protein RRMs. The peptides display mild selectivities with respect to the binding of the different homooligomers. Binding studies in 500 mM magnesium chloride suggest that the complex formation is not predominantly driven by Coulombic attraction. These peptides represent a starting point for further studies of non-Coulombic binding of RNA by peptides and proteins, which is important in the context of contemporary biology, potential therapeutic applications, and prebiotic peptide-RNA interactions.
引用
收藏
页码:243 / 248
页数:6
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