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Beta-peptides: twisting and turning.

K Gademann1, T Hintermann, J V Schreiber

  • 1Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule Zürich, Universitätstr. 16, ETH Zentrum, Zürich, CH-8092, Switzerland. gademann@org.chem.ethz.ch

Current Medicinal Chemistry
|October 16, 1999
PubMed
Summary

Beta-peptides, readily synthesized, adopt diverse secondary structures like helices and hairpins. These stable peptidomimetics show resistance to enzymatic degradation and mimic natural hormones, offering therapeutic potential.

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Area of Science:

  • Peptide Chemistry
  • Biochemistry
  • Structural Biology

Background:

  • Beta-peptides are oligomers of beta-amino acids, offering a versatile scaffold for novel molecular structures.
  • They are readily synthesized using standard methods in solution and on solid support.
  • Beta-peptides are recognized as promising peptidomimetics due to their unique properties.

Purpose of the Study:

  • To investigate the diverse secondary structures adopted by beta-peptides in solution and solid states.
  • To explore the stability and folding pathways of beta-peptide helices and other conformations.
  • To evaluate the potential of beta-peptides as therapeutic agents and biomimetic molecules.

Main Methods:

  • Two-dimensional NMR spectroscopy to elucidate secondary structures (e.g., 314 helix, hairpin).

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  • CD spectroscopy to assess thermal stability of helical structures.
  • Molecular Dynamics (MD) simulations to observe reversible peptide folding and identify pathways.

    • Main Results:

    • Beta-peptides 4, 5, and 10 form stable, thermally robust left- or right-handed 314 helices.
    • A novel helix with 12- and 10-membered turns was identified in mixed beta-peptide 8.
    • NMR studies revealed a hairpin structure for beta-peptide 21, and MD simulations demonstrated reversible folding.
    • Beta-peptides exhibit resistance to proteolytic enzymes and possess favorable pharmacokinetic properties (e.g., long half-lives).
    • Beta-peptide conjugates act as efficient ligands for HLA*B27, and cyclic beta-peptides mimic somatostatin activity.

    Conclusions:

    • Beta-peptides readily form diverse, stable secondary structures including helices and hairpins.
    • They demonstrate significant resistance to enzymatic degradation and possess favorable stability.
    • Beta-peptides show promise as peptidomimetics, capable of mimicking natural hormones and acting as ligands for MHC proteins.