Cyclization of a G4-specific peptide enhances its stability and G-quadruplex binding affinity. Issue 7 (2nd January 2020)

• Record Type: Journal Article
• Authors: Ngo, Khac Huy; Yang, Renliang; Das, Poulomi; Nguyen, Giang K. T.; Lim, Kah Wai; Tam, James P.; Wu, Bin; Phan, Anh Tuân
• Is Part Of: Chemical communications. Volume 56:Issue 7(2020)
• Page Start: 1082
• Page End: 1084
• Publication Date: 2020-01-02
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c9cc06748e
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Head-to-tail cyclization of a G-quadruplex-specific peptide was shown to enhance its stability and G-quadruplex binding affinity. 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.