The study on helix-inducing propensity of A-hydroxymethylserine based on the host-guest approach

• Autorzy: Lisowski M. , Stasiak M. , Leplawy M.
• Języki publikacji: EN

Abstrakty

EN

The solid phase synthesis of a-hydroxymethylserine peptides is affected by accumulation of deleted sequences and NŽO-acyl migrations, occurring under acidic conditions of cleavage from Wang resin. The conformational behaviour of peptides, containing alanine host-residues separated by a single or consecutive a-hydroxymethylserine (HmS) guest-residues, has been studied by CD spectroscopy in polar protic solvents. The presence of sequential motif (Ala-HmS)n, n=2,4, shifts the conformational equilibria towards ordered structures. The CD spectrum of the nonapeptide Ac-Ala-(HmS-Ala)4-OH in trifluoroethanol is indicative of a right-handed helix. Peptides with consecutive HmSn residues, n=2,3, are apparently less ordered than those containing alternating sequences Ala-HmS. Random coil conformation is adopted by the nonapeptide Ac-Ala3-(HmS)3-Ala-OH containing three neighbouring HmS residues.

Słowa kluczowe

EN

A-hydroxymethylserine; A-disubstituted amino acids; peptide conformation; CD spectroscopy; amino acid fluorides; N→O-acyl migration

• Wydawca: Polskie Towarzystwo Chemiczne
• Czasopismo: Polish Journal of Chemistry
• Rocznik: 1999
• Tom: vol. 73 nr 2
• Strony: 313--319

Twórcy

autor

Lisowski M.

autor

Stasiak M.

autor

Leplawy M.

• Wydział Chemii Uniwersytet Wrocławski ul. F. Joliot-Curie 14 50-383 Wrocław