Conformational analysis of sugar-peptide adducts in the solution state by NMR spectroscopy and molecular modelling (CROSBI ID 180728)
Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Jerić, Ivanka ; Novak, Predrag ; Vinković, Mladen ; Horvat, Štefica
engleski
Conformational analysis of sugar-peptide adducts in the solution state by NMR spectroscopy and molecular modelling
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.
NMR spectroscopy ; molecular modelling ; sugar–peptide adducts
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Podaci o izdanju
(10)
2001.
1944-1950
objavljeno
1472-779X
1364-5471
10.1039/b104239b
Povezanost rada
Kemija