Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/143224
Title: Stapling a G-quadruplex specific peptide
Authors: Yaneva, Militsa Yavorova
Cheong, Vee Vee
Cheng, Jun Kee
Lim, Kah Wai
Phan, Anh Tuân
Keywords: Science::Biological sciences
Science::Chemistry
Issue Date: 2020
Source: Yaneva, M. Y., Cheong, V. V., Cheng, J. K., Lim, K. W., & Phan, A. T. (2020). Stapling a G-quadruplex specific peptide. Biochemical and Biophysical Research Communications. doi:10.1016/j.bbrc.2020.02.144
Project: NRF-NRFI2017-09
MOE2018- T2-2-029
Journal: Biochemical and Biophysical Research Communications
Abstract: G-quadruplex (G4) is a non-canonical four-stranded nucleic acid structure and the RHAU helicase has been identified to have high specificity for recognition of parallel-stranded G4s. We have designed and synthesized two stapled peptide analogues of the G4-specfic motif of RHAU, which preserve the G4 binding ability. Characterization of these peptides identified the stapled variants to exhibit higher helical formation propensity in aqueous buffer in comparison to the native RHAU sequence. Moreover, the stapled peptides exhibit superior enzymatic stability towards α-chymotrypsin. Our stapled RHAU peptides can serve as a new tool for targeting G4 nucleic acid structures.
URI: https://hdl.handle.net/10356/143224
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2020.02.144
Rights: © 2020 Elsevier Inc. All rights reserved. This paper was published in Biochemical and Biophysical Research Communications and is made available with permission of Elsevier Inc.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Journal Articles

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