Cited by 45Supramolecular Chemistry and ComplexesChemical Synthesis and AnalysisProtein Structure and Dynamics

Inducing α-Helices in Short Oligopeptides through Binding by an Artificial Hydrophobic Cavity

Dolain, Christel, Hatakeyama, Yoshiyuki, Sawada, Tomohisa, Tashiro, Shohei, Fujita, Makoto·2010·Journal of the American Chemical Society

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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Crossref · 10.1021/ja100585w

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29 of 29 references verified0 citation errors · 0 not checkable

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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
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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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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