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Turn conformations in peptides containing the -Xaa-Ser- sequence

R A Shaw1, A Perczel, G D Fasman

  • 1Institute for Biodiagnostics, National Research Council of Canada, Winnipeg, Manitoba, Canada.

International Journal of Peptide and Protein Research
|July 1, 1996
PubMed
Summary
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Protected dipeptides adopt specific beta-turn conformations in solution, influenced by amino acid sequence and solvent. Infrared spectroscopy revealed distinct hydrogen bonding patterns crucial for stabilizing these peptide structures.

Area of Science:

  • * Structural chemistry
  • * Spectroscopy
  • * Peptide chemistry

Background:

  • * Understanding peptide conformations is crucial for drug design and biomaterials.
  • * Beta-turns are important secondary structures in peptides and proteins.
  • * The role of specific amino acid residues, like serine, in stabilizing these structures requires further investigation.

Purpose of the Study:

  • * To investigate the solution conformations of four protected dipeptides: Boc-L-Pro-L-Ser-NHMe, Boc-L-Pro-D-Ser-NHMe, Boc-L-Val-L-Ser-NHMe, and Boc-L-Val-D-Ser-NHMe.
  • * To elucidate the influence of solvent (CH2Cl2, DMSO, D2O) on peptide conformation and hydrogen bonding.
  • * To explore the role of the serine residue in stabilizing beta-turn structures.

Main Methods:

  • * Infrared (IR) spectroscopy was employed to analyze peptide conformations in different solvents.

Related Experiment Videos

  • * Characteristic shifts in urethane C=O and terminal NH stretching frequencies indicated beta-turn formation.
  • * Amide I absorption patterns were analyzed to differentiate between beta-turn types (I and II) and assess hydrogen bonding.

    • Main Results:

    • * All four protected dipeptides formed ten-membered ring beta-turns in CH2Cl2 solution.
    • * LL and LD isomers exhibited distinct amide I absorption patterns, consistent with type I and type II beta-turns, respectively.
    • * Intramolecular hydrogen bonding was disrupted in DMSO, and intermolecular hydrogen bonding was absent in aqueous solutions.
    • * The serine hydroxyl group participated in hydrogen bonding to the serine carbonyl group, with additional free OH groups observed.

    Conclusions:

    • * Protected dipeptides Boc-L-Pro-L-Ser-NHMe, Boc-L-Pro-D-Ser-NHMe, Boc-L-Val-L-Ser-NHMe, and Boc-L-Val-D-Ser-NHMe adopt specific beta-turn conformations in solution.
    • * Solvent polarity significantly impacts hydrogen bonding and the stability of these conformations.
    • * The serine residue plays a role in stabilizing beta-turn structures through hydrogen bonding.