Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity
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 c...
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sg-ntu-dr.10356-1505402023-02-28T17:10:55Z Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity Ngo, Khac Huy Yang, Renliang Das, Poulomi Nguyen, Giang Kien Truc Lim, Kah Wai Tam, James P. Wu, Bin Phan, Anh Tuân School of Physical and Mathematical Sciences School of Biological Sciences NTU Institute of Structural Biology Science::Chemistry::Biochemistry Science::Biological sciences Guanine Quadruplex Membrane Protein 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 Ministry of Education (MOE) Submitted/Accepted version This work was supported by Singapore Ministry of Education (MOE) Academic Research Fund Tier 2 (MOE2018-T2-2-029) to A. T. P. and MOE Academic Research Fund Tier 3 (MOE2016-T3- 1-003) to J. P. T 2022-05-18T02:51:18Z 2022-05-18T02:51:18Z 2020 Journal Article 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 1359-7345 https://hdl.handle.net/10356/150540 10.1039/C9CC06748E 7 56 1082 1084 en MOE2018-T2-2-029 MOE2016-T3-1-003 Chemical Communications © 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. application/pdf |
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Science::Chemistry::Biochemistry Science::Biological sciences Guanine Quadruplex Membrane Protein Ngo, Khac Huy Yang, Renliang Das, Poulomi Nguyen, Giang Kien Truc Lim, Kah Wai Tam, James P. Wu, Bin Phan, Anh Tuân Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity |
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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 |
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School of Physical and Mathematical Sciences |
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School of Physical and Mathematical Sciences Ngo, Khac Huy Yang, Renliang Das, Poulomi Nguyen, Giang Kien Truc Lim, Kah Wai Tam, James P. Wu, Bin Phan, Anh Tuân |
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Article |
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Ngo, Khac Huy Yang, Renliang Das, Poulomi Nguyen, Giang Kien Truc Lim, Kah Wai Tam, James P. Wu, Bin Phan, Anh Tuân |
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Ngo, Khac Huy |
title |
Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity |
title_short |
Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity |
title_full |
Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity |
title_fullStr |
Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity |
title_full_unstemmed |
Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity |
title_sort |
cyclization of a g4-specific peptide enhances its stability and g-quadruplex binding affinity |
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2022 |
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https://hdl.handle.net/10356/150540 |
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1759854024975187968 |