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Article

Exploring the Interactions Between RHAU Peptide and G-Quadruplex Dimers Based on Chromatographic Retention Behaviors

by
Ju Wang
1,
Jun-Qin Qiao
1,*,
Chao Liang
2,
Xue-Wen Guo
1,
Meng-Ying Zhang
2,*,
Wei-Juan Zheng
3 and
Hong-Zhen Lian
1,*
1
State Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry & Chemical Engineering and Center of Materials Analysis, Nanjing University, 163 Xianlin Avenue, Nanjing 210023, China
2
Nanjing Zhulu Pharmaceutical Technology Co., Ltd., 28 Kexin Road, Nanjing 211500, China
3
State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, 163 Xianlin Avenue, Nanjing 210023, China
*
Authors to whom correspondence should be addressed.
Molecules 2024, 29(24), 5915; https://doi.org/10.3390/molecules29245915
Submission received: 25 October 2024 / Revised: 9 December 2024 / Accepted: 12 December 2024 / Published: 14 December 2024
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Abstract

G-quadruplex (G4), an important secondary structure of nucleic acids, is polymorphic in structure. G4 monomers can associate with each other to form multimers, which show better application performance than monomers in some aspects. G4 dimers, the simplest and most widespread multimeric structures, are often used as a representative for studying multimers. RHAU, a G4 ligand, has been reported to recognize G4 dimers. However, there are few reports focusing on interactions between RHAU and different G4 dimers. In this work, interactions between RHAU peptide and six G4 dimers were investigated by size-exclusion chromatography (SEC). It was revealed that compared to the hybrid G4 monomer, the hybrid tandem unstacked G4 dimer could form special binding sites, leading to a weak interaction with RHAU. It was also found that the steric hindrance at terminal G-tetrads of a special Z-G4 structure greatly weakened their interactions with RHAU. Additionally, RHAU exhibited stronger interactions with intermolecular stacked/interlocked parallel dimers than with intramolecular tandem stacked parallel dimers. This work enriches the understanding of interactions between RHAU and G4 dimers, which is conducive to the elucidation of G4 polymorphism, and provides a strong reference for studying G4 multimer–peptide interactions.
Keywords: size-exclusion chromatography; SEC; G-quadruplex dimers; G4 dimer–RHAU interaction; retention behavior size-exclusion chromatography; SEC; G-quadruplex dimers; G4 dimer–RHAU interaction; retention behavior

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MDPI and ACS Style

Wang, J.; Qiao, J.-Q.; Liang, C.; Guo, X.-W.; Zhang, M.-Y.; Zheng, W.-J.; Lian, H.-Z. Exploring the Interactions Between RHAU Peptide and G-Quadruplex Dimers Based on Chromatographic Retention Behaviors. Molecules 2024, 29, 5915. https://doi.org/10.3390/molecules29245915

AMA Style

Wang J, Qiao J-Q, Liang C, Guo X-W, Zhang M-Y, Zheng W-J, Lian H-Z. Exploring the Interactions Between RHAU Peptide and G-Quadruplex Dimers Based on Chromatographic Retention Behaviors. Molecules. 2024; 29(24):5915. https://doi.org/10.3390/molecules29245915

Chicago/Turabian Style

Wang, Ju, Jun-Qin Qiao, Chao Liang, Xue-Wen Guo, Meng-Ying Zhang, Wei-Juan Zheng, and Hong-Zhen Lian. 2024. "Exploring the Interactions Between RHAU Peptide and G-Quadruplex Dimers Based on Chromatographic Retention Behaviors" Molecules 29, no. 24: 5915. https://doi.org/10.3390/molecules29245915

APA Style

Wang, J., Qiao, J.-Q., Liang, C., Guo, X.-W., Zhang, M.-Y., Zheng, W.-J., & Lian, H.-Z. (2024). Exploring the Interactions Between RHAU Peptide and G-Quadruplex Dimers Based on Chromatographic Retention Behaviors. Molecules, 29(24), 5915. https://doi.org/10.3390/molecules29245915

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