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Related Experiment Videos

Intramolecular ditryptophan crosslinks enforce two types of antiparallel beta structures.

J H Matthews1, T D Dinh, P Tivitmahaisoon

  • 1Department of Chemistry, University of California, Irvine, CA 92697-2025, USA.

Chemistry & Biology
|December 4, 2001
PubMed
Summary

Ditryptophan crosslinks, similar to disulfide bonds, influence peptide structure. These biaryl crosslinks favor antiparallel beta-sheet formation in peptides, particularly when hydrogen bonding is optimized.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Peptide Chemistry

Background:

  • Two natural biaryl crosslinks, ditryptophan and dityrosine, can form in proteins.
  • Biaryl crosslinks share topology with disulfide crosslinks.
  • The impact of biaryl crosslinks on local peptide structure remains largely uncharacterized.

Purpose of the Study:

  • To investigate the structural effects of ditryptophan crosslinks in model peptides.
  • To determine if ditryptophan crosslinks influence secondary structure formation.

Main Methods:

  • Synthesis of three ditryptophan-linked peptide dimers with varying termini (Ac-Leu-Trp-Ala-COX).
  • Crystallization and structural analysis of the peptide dimers.
  • Solubility assessment of different peptide dimer derivatives.

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Main Results:

  • One tripeptide dimer derivative was insoluble.
  • A ditryptophan-linked peptide dimer with methyl ester termini crystallized as an antiparallel beta-sheet.
  • Another dimer derivative adopted a slipped antiparallel beta structure.

Conclusions:

  • Intermolecular ditryptophan crosslinks can promote antiparallel beta-sheet structures in peptides.
  • The preference for antiparallel beta-sheet structure is enhanced by optimal hydrogen bonding capabilities at the dimer edges.