Depsipeptide analogues of elastin repeating sequences: synthesis.
Depsipeptide analogues of peptide sequences can help in elucidating the role of specific hydrogen bonds in determining the conformation in peptides. The repeating pentapeptide and hexapeptide sequences of elastin have been suggested to contain a type II beta-turn with a 4----1 hydrogen bond. Depsipeptide analogues of the repeating sequences of elastin in which this 4----1 hydrogen bond cannot exist were synthesized. A fragment condensation approach was employed in which the depsipeptide ester bond was introduced early in the synthesis. This approach proved to be effective, although the increased lability of the depsipeptide ester bond resulted in side products and low yields in some reactions.
Arad
O
O
Chemistry Department, University of California, San Diego, La Jolla 92093.
Goodman
M
M
D000595:Amino Acid Sequence; D004121:Dimethyl Sulfoxide; D004549:Elastin / Q000031:analogs & derivatives / Q000138:chemical synthesis; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009842:Oligopeptides / Q000138:chemical synthesis; D011487:Protein Conformation
D009842:Oligopeptides; D004549:Elastin; D004121:Dimethyl Sulfoxide