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Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity

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Abstract

G-quadruplexes (G4) are non-canonical nucleic acid structures with important implications in biology. Based on an α-helical fragment of the RHAU helicase that displays high specificity for parallel-stranded G-quadrplexes, herein we demonstrate its head-to-tail cyclization by a high-efficiency ligase. The cyclic peptide exhibits superior stability and binding affinity to a G-quadruplex, and can serve as an excellent investigational tool for chemical biology applications.

Graphical abstract: Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity

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Article information


Submitted
30 Aug 2019
Accepted
05 Dec 2019
First published
02 Jan 2020

Chem. Commun., 2020, Advance Article
Article type
Communication

Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity

K. H. Ngo, R. Yang, P. Das, G. K. T. Nguyen, K. W. Lim, J. P. Tam, B. Wu and A. T. Phan, Chem. Commun., 2020, Advance Article , DOI: 10.1039/C9CC06748E

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