Stapling a G-quadruplex specific peptide

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2020-10, Vol.531 (1), p.62-66
Main Authors: Yaneva, Militsa Yavorova, Cheong, Vee Vee, Cheng, Jun Kee, Lim, Kah Wai, Phan, Anh Tuân
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Binding Sites
DEAD-box RNA Helicases - chemical synthesis
DEAD-box RNA Helicases - chemistry
DEAD-box RNA Helicases - metabolism
G-quadruplex
G-quadruplex-binding protein
G-Quadruplexes
Humans
Models, Molecular
Peptides - chemical synthesis
Peptides - chemistry
Peptides - metabolism
Protein Binding
Protein Conformation, alpha-Helical
RHAU helicase
Stapled peptides
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2020.02.144