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Self-Assembling Amphiphiles for Construction of Protein Molecular Architecture

Yu, Ying-Ching, Berndt, Peter, Tirrell, Matthew, Fields, Gregg B.·1996·Journal of the American Chemical Society

Abstract

Peptide-amphiphiles with collagen-model head groups and dialkyl chain tails have been synthesized and shown to self-assemble into highly ordered polyPro II like triple-helical structures when dissolved in aqueous subphases. Evidence for this self-assembly process has been obtained from (a) compression of stable peptide-amphiphile monolayers to molecular areas comparable with triple-helical areas, (b) circular dichroism spectra and melting curves characteristic of triple-helices, and (c) two-dimensional NMR spectra indicative of stable triple-helical structure at low temperatures and melted triple-helices at high temperatures. The thermal stability of the collagen-like structure in the peptide-amphiphile is substantially higher (Δ T m = 15−20 °C) than that of peptides without lipidation. The assembly process driven by the hydrophobic tail may provide a general method for creating well-defined protein molecular architecture using a minimalist peptide-based approach.

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Metadata

Authors
Yu, Y.-C., Berndt, P., Tirrell, M., & Fields, G. B.
Venue
Journal of the American Chemical Society
Published
1996-01-01
Volume
118
Issue
50
Pages
12515-12520
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
OpenAlex
W2055628427
Cited by
265
References
0
FWCI
3.63
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Self-Assembling Amphiphiles for Construction of Protein Molecular Architecture. https://app.cochat.ai/papers/10.1021/ja9627656
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Yu, Y.-C., Berndt, P., Tirrell, M., & Fields, G. B. (1996). Self-Assembling Amphiphiles for Construction of Protein Molecular Architecture. Journal of the American Chemical Society. https://doi.org/10.1021/ja9627656

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