Study on the Interaction of a Peptide Targeting Specific G-Quadruplex Structures Based on Chromatographic Retention Behavior

G-quadruplexes (G4s) are of vital biological significance and G4-specific ligands with conformational selectivity show great application potential in disease treatment and biosensing. RHAU, a RNA helicase associated with AU-rich element, exerts biological functions through the mediation of G4s and h...

Full description

Saved in:
Bibliographic Details
Published in:International journal of molecular sciences 2023-01, Vol.24 (2), p.1438
Main Authors: Wang, Ju, Qiao, Junqin, Zheng, Weijuan, Lian, Hongzhen
Format: Article
Language:English
Subjects:
Binding
Biosensors
Chromatography
Circular dichroism
conformational selectivity
DEAD-box RNA Helicases - metabolism
Dichroism
DNA helicase
Electrophoresis
G-Quadruplexes
G4-peptide interaction
Gel electrophoresis
Gene expression
Investigations
Ligands
Peptides
Peptides - chemistry
Polyacrylamide
Polymorphism
Retention
retention behavior
RNA helicase
Selectivity
Size exclusion chromatography
Structural analysis
Ultraviolet absorption
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:G-quadruplexes (G4s) are of vital biological significance and G4-specific ligands with conformational selectivity show great application potential in disease treatment and biosensing. RHAU, a RNA helicase associated with AU-rich element, exerts biological functions through the mediation of G4s and has been identified to be a G4 binder. Here, we investigated the interactions between the RHAU peptide and G4s with different secondary structures using size exclusion chromatography (SEC) in association with circular dichroism (CD), ultraviolet-visible (UV-Vis) absorption, and native polyacrylamide gel electrophoresis (Native-PAGE). Spectral results demonstrated that the RHAU peptide did not break the main structure of G4s, making it more reliable for G4 structural analysis. The RHAU peptide was found to display a structural selectivity for a preferential binding to parallel G4s as reflected by the distinct chromatographic retention behaviors. In addition, the RHAU peptide exhibited different interactions with intermolecular parallel G4s and intramolecular parallel G4s, providing a novel recognition approach to G4 structures. The findings of this study enriched the insight into the binding of RHAU to G4s with various conformations. It is noteworthy that SEC technology can be easy and reliable for elucidating G4-peptide interactions, especially for a multiple G4 coexisting system, which supplied an alternative strategy to screen novel specific ligands for G4s.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms24021438