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

• Published in: International journal of molecular sciences Vol. 24; no. 2; p. 1438
• Main Authors: Wang, Ju, Qiao, Junqin, Zheng, Weijuan, Lian, Hongzhen
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 11.01.2023; MDPI
• 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; G4-peptide interaction; G-quadruplexes; conformational selectivity; retention behavior; size exclusion chromatography
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms24021438

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.