ArticleChemical science2023
Modulating the folding and binding of peptides using a stimuli-responsive molecular tweezer.
Article in Chemical science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Enhancement of Structural Stability and IgG Affinity of aAntibodies (Basel, Switzerland) · 2025Article
- Antioxidant Peptide-Based Nanocarriers for Delivering Wound Healing Agents.Tissue engineering and regenerative medicine · 2025Article
- Self-assembling biomolecules for biosensor applications.Biomaterials research · 2023Review
Corrections and comments
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Authors and funding
9 authors.
Funding
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Abstract
This study presents the development of a β-hairpin (tryptophan zipper, Trpzip)-based molecular tweezer (MT) that can control the folding and binding of α-helical peptides. When an α-helix isolated from the p53 protein was conjugated with Trpzip in an optimized macrocyclic structure, the folded β-hairpin stabilized the helix conformation through the side chain-to-side chain stapling strategy, which notably enhanced target (hDM2) affinity of the peptide. On the other hand, the helicity and binding affinity were significantly reduced when the hairpin was unfolded by a redox stimulus. This stimulus-responsive property was translated into the effective capture and release of model multivalent biomaterials, hDM2-gold nanoparticle conjugates. Since numerous protein interactions are mediated by α-helical peptides, these results suggest that the β-hairpin-based MT holds great potential to be utilized in various biomedical applications, such as protein interaction inhibition and cancer biomarker (
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Registered trials
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