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Discovery and characterization of a high-affinity G-quadruplex binding peptide via mRNA display
Naka Kudo Ida1, Yoshimasa Kawaguchi1, Shiroh Futaki2
1Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.
Bioorganic & Medicinal Chemistry
|January 14, 2026
Summary
Researchers developed a novel G-quadruplex (G4)-binding peptide, LP7, using mRNA display. This peptide effectively targets G4 structures, showing potential for therapeutic applications in G4-related diseases.
Area of Science:
- Molecular Biology
- Biochemistry
- Drug Discovery
Background:
- G-quadruplexes (G4s) are non-canonical nucleic acid structures vital for gene regulation.
- Dysregulation of G4s is linked to various diseases, necessitating G4-binding molecules for therapeutic intervention.
Purpose of the Study:
- To develop novel G4-binding peptides with high affinity using directed evolution.
- To characterize the binding properties and therapeutic potential of the identified peptide.
Main Methods:
- Utilized mRNA display technology for directed evolution to discover G4-binding peptides.
- Performed binding assays, including affinity measurements (Kd) for the identified peptide (LP7).
- Conducted sequence-activity relationship analysis and functional assays to assess inhibitory effects on reverse transcription.
Main Results:
- Identified a novel peptide, LP7, with high affinity and preference for parallel G4 structures.
- Dimerization of LP7 enhanced binding to hTERC rG4 by 70-fold (Kd = 7 nM).
- LP7 demonstrated G4-dependent inhibition of reverse transcription, with basic and aromatic residues being critical for binding.
Conclusions:
- mRNA display is an effective platform for discovering G4-binding peptides.
- LP7 shows promise as a therapeutic tool for modulating G4-mediated gene functions.
- Detailed characterization of LP7 offers insights into G4 recognition mechanisms for future drug development.
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