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Related Experiment Videos

Depsipeptide analogues of elastin repeating sequences: conformational analysis.

O Arad1, M Goodman

  • 1Chemistry Department, University of California, San Diego, La Jolla 92093.

Biopolymers
|October 1, 1990
PubMed
Summary

Eliminating a specific hydrogen bond in elastin peptides, like Val-Pro-Gly-Val-Gly, shifts their structure from beta-turns to gamma-turns. This conformational change impacts elastin

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Area of Science:

  • Biochemistry
  • Polymer Science
  • Structural Biology

Background:

  • Elastin's repeating sequences, such as pentapeptide Val-Pro-Gly-Val-Gly and hexapeptide Val-Ala-Pro-Gly-Val-Gly, are crucial for its elastic properties.
  • These sequences are proposed to adopt a beta-turn conformation stabilized by a specific hydrogen bond.

Purpose of the Study:

  • To investigate the conformational impact of eliminating a key hydrogen bond in elastin's repeating peptide sequences.
  • To compare the structures of peptide analogues with their depsipeptide counterparts where the hydrogen bond is absent.

Main Methods:

  • Synthesis of peptide and depsipeptide analogues, including Val-Pro-Gly-Hiv-Gly and Val-Ala-Pro-Gly-Hiv-Gly (Hiv: S-alpha-hydroxyisovaleric acid).
  • Conformational analysis using nuclear magnetic resonance (NMR), circular dichroism (CD), and infrared (IR) spectroscopy.

Related Experiment Videos

  • Study of derivatives with various protecting groups and end groups, as well as polymers.

    • Main Results:

    • Depsipeptide analogues, lacking the specific 4-1 beta-turn hydrogen bond, predominantly exhibit a gamma-turn structure.
    • Peptide sequences show an equilibrium between gamma-turn and beta-turn structures in the Pro-Gly segment.
    • N-methylamide derivatives display a similar equilibrium in the Gly-Val-Gly segment.

    Conclusions:

    • The specific hydrogen bond is critical for the formation of beta-turns in elastin's repeating sequences.
    • An equilibrium between gamma-turns and beta-turns contributes to elastin's combined flexibility and conformational preference.
    • In depsipeptides, the absence of the beta-turn allows for the observation of gamma-turns, while polydepsipeptides show a preference for type I beta-turns.