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 | Schools: | School of Physical and Mathematical Sciences | Organisations: | NTU Institute of Structural Biology | 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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