Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/150540
Title: Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity
Authors: Ngo, Khac Huy
Yang, Renliang
Das, Poulomi
Nguyen, Giang Kien Truc
Lim, Kah Wai
Tam, James P.
Wu, Bin
Phan, Anh Tuân
Keywords: Science::Chemistry::Biochemistry
Science::Biological sciences
Issue Date: 2020
Source: Ngo, K. H., Yang, R., Das, P., Nguyen, G. K. T., Lim, K. W., Tam, J. P., Wu, B. & Phan, A. T. (2020). Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity. Chemical Communications, 56(7), 1082-1084. https://dx.doi.org/10.1039/C9CC06748E
Project: MOE2018-T2-2-029
MOE2016-T3-1-003
Journal: Chemical Communications
Abstract: G-quadruplexes(G4) arenon-canonical nucleicacidstructures with important implications in biology. Based on an a-helical fragment of the RHAU helicase that displays high specificity for parallelstranded 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
URI: https://hdl.handle.net/10356/150540
ISSN: 1359-7345
DOI: 10.1039/C9CC06748E
Rights: © 2020 The Royal Society of Chemistry. All rights reserved. This paper was published in Chemical Communications and is made available with permission of The Royal Society of Chemistry.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles
SPMS Journal Articles

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