Naslov
Conformational analysis of sugar-peptide adducts in the solution state by NMR spectroscopy and molecular modelling

Autori
Jerić, Ivanka ; Novak, Predrag ; Vinković, Mladen ; Horvat, Štefica

Izvornik
Journal of the Chemical Society. Perkin Transactions 2 (2001) (1472-779X) (2001), 10; 1944-1950

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
NMR spectroscopy ; molecular modelling ; sugar–peptide adducts

Sažetak
A combined use of NMR spectroscopy and molecular modelling has enabled insight into conformational features of the novel sugar–peptide adducts 1–3. Cyclic neoglycopeptide 1, having the β--glucopyranose moiety which connects terminal parts of the Tyr-Pro-Phe sequence into a 14-membered ring, has been found in a rigid conformation with a sandwich-like arrangement of the proline residue flanked by the tyrosine and the phenylalanine side-chains. However, cyclic Tyr-Pro-Phe-Val-related Amadori compound 2, with an 18-membered glycopeptide ring, has shown more flexibility in the peptide backbone and amino acid side-chains. Nevertheless, mutarotation was obstructed and the 1-deoxy--fructofuranose moiety was found in the β configuration exclusively. The analysis of the Amadori compound 3, with an unsubstituted C-terminal of the Tyr-Pro-Phe-Val peptide, has revealed the presence of conformational isomers arising from trans–cis isomerism of the Tyr1-Pro2 peptide bond, while the 1-deoxy--fructose has been found in the β-pyranose form. The results presented here point towards peptide sequence-governed overall conformation of the studied neoglycopeptides.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA