Inducing α-Helices in Short Oligopeptides through Binding by an Artificial Hydrophobic Cavity
Abstract
Short peptides were induced into alpha-helix conformations in water through enclathration to an artificial hydrophobic cavity. Peptides with two aromatic residues showed high affinity for the host, and these intermolecular aromatic-aromatic interactions specifically drove the helical folding of short peptides.
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Modulators of Protein–Protein Interactions
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- Authors
- Dolain, C., Hatakeyama, Y., Sawada, T., Tashiro, S., & Fujita, M.
- Affiliations
- Japan Science and Technology Agency (JP)
- Corresponding author
- Fujita, Makoto
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-04-01
- Volume
- 132
- Issue
- 16
- Pages
- 5564-5565
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1996659972
- Cited by
- 45
- References
- 29
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 4 · 2023: 2 · 2022: 1 · 2021: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 2 · 2015: 6 · 2014: 2 · 2013: 5 · 2012: 7
- FWCI
- 3.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of the American Chemical Society (publishedVersion)
- PubMed (publishedVersion)
- Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Supramolecular Chemistry and Complexes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- host-guest complexation, enclathration, aromatic-aromatic interactions, peptide folding, host-guest chemistry
- MeSH terms
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Oligopeptides, Protein Binding, Water, Protein Structure, Secondary, Protein Folding, Hydrophobic and Hydrophilic Interactions
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