Harnessing D-amino acids for peptide motif designs. Synthesis and solution conformation of Boc-D-Glu-Ala-Gly-Lys-NHMe and Boc-L-Glu-Ala-Gly-Lys-NHMe

Int J Pept Protein Res. 1994 Mar;43(3):209-18.

Abstract

In examining the use of D-amino acids in designing specific peptide folding motifs, the tetrapeptide Boc-D-Glu-Ala-Gly-Lys-NHMe 1 and its analog 2 featuring L-Glu were synthesized for a comparison of their solution conformations by NMR spectroscopy. The temperature coefficients of amide proton resonances, NOE data, side-chain CH2 anisotropies and salt titration results suggest a weak type II reverse-turn conformation for peptide 2, and a tandem II' turn-3(10)-helix conformation of appreciable conformational stability for peptide 1 in apolar solvents. The latter is of potential interest as the N-terminal helix cap that could support the design of longer 3(10) helices. Possible origins of appreciable difference in the conformational stabilities of the diastereomers are discussed.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry*
  • Drug Stability
  • Magnetic Resonance Spectroscopy / methods
  • Molecular Sequence Data
  • Peptides / chemical synthesis*
  • Peptides / chemistry*
  • Protein Conformation
  • Protein Folding
  • Sensitivity and Specificity
  • Solutions
  • Stereoisomerism
  • Temperature

Substances

  • Amino Acids
  • Peptides
  • Solutions