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Related Experiment Videos

Long, chiral polypeptide 3(10)-helices at atomic resolution.

A Bavoso1, E Benedetti, B Di Blasio

  • 1Department of Chemistry, University of Napoli, Italy.

Journal of Biomolecular Structure & Dynamics
|February 1, 1988
PubMed
Summary

Short peptides rich in alpha-aminoisobutyric acid (Aib) form stable right-handed 3(10)-helices. This helical structure, confirmed by X-ray diffraction, is crucial for understanding ion-transporting peptaibol antibiotics.

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Area of Science:

  • Peptide Chemistry
  • Structural Biology
  • Biophysics

Background:

  • Short peptides, particularly those rich in alpha-aminoisobutyric acid (Aib), are known for their propensity to form helical structures.
  • Understanding the conformational preferences of these peptides is essential for deciphering the mechanisms of membrane-active antibiotics.

Purpose of the Study:

  • To determine the crystal-state preferred conformation of terminally blocked hepta- and octapeptides containing Aib residues.
  • To investigate the role of the single L-residue in dictating the helical screw sense.
  • To provide atomic-resolution insights into larger 3(10)-helical structures.

Main Methods:

  • X-ray diffraction analysis of terminally blocked hepta- and octapeptides with the general formula -(Aib)n L-Leu-(Aib)2- (n = 4 and 5).

Related Experiment Videos

  • Analysis of intramolecular hydrogen bonding patterns (C(10)-III type).

    • Main Results:

    • The hepta- and octapeptides adopt right-handed 3(10)-helical conformations.
    • These helices are stabilized by five and six consecutive intramolecular NH...O = C H-bonds, respectively.
    • The octapeptide structure is the first atomic-resolution observation of a regular, chiral 3(10)-helix exceeding two turns.
    • The internal L-residue dictates the right-handed screw sense of both helices.

    Conclusions:

    • Short peptides rich in Aib exhibit a strong propensity to form 3(10)-helical structures.
    • The findings enhance the understanding of conformational preferences in peptaibol antibiotics.
    • This structural data is valuable for studying channel-forming and ion-transporting peptides.