Isomerization of the Xaa-Pro peptide bond induced by ionic interactions of arginine (Journal article)
Tsikaris, V./ Sakarellos-Daitsiotis, M./ Tzovaras, D./ Sakarellos, C./ Orlewski, P./ Cung, M. T./ Marraud, M.
Inclusion of Arg or Pro residues in proteins and peptides has been proved to play an essential role in biochemical functions through ionic interactions, conformational transitions, and formation of turns as well. In this study we present the conformational properties of the Ac-Arg-Ala-Pro (1), Ac-Arg-Ala-Pro-NH2 (2), Ac-Arg-Pro-Asp-NH2 (3), and Ac-Arg-Pro-Asp (4) tripeptides peptides, using H-1-nmr spectroscopy and molecular dynamics. These peptides were, modeled with the aim of studying the role of the Arg-guanidinium to carboxylate ionic interactions on the Xaa-Pro peptide bond isomerization. It was found with I and 4 that arginine preferentially interacts with the C-terminal carboxylate group, even though the beta-carboxylate is also accessible. This tendency of the Arg moiety was found to induce the cis disposition of the Ala-Pro peptide bond in I, It was also confirmed that the Arg ... Asp side chain-side chain ionic interactions in 3 plays a key role in backbone folding and structural stabilization through a type I beta-turn. The nmr pattern for 3 showed a remarkable similarity with that for various Arg-Tyr-Asp containing peptides, a sequence that is crucial for the adhesion properties of the Leishmania gp63 glycoprotein. (C) 1996 John Wiley & Sons, Inc.
|Institution and School/Department of submitter:||Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας|
|Keywords:||turn conformations,reverse turns,arg,sequence,proteins,nmr,fibrinogen,receptor,h-1-nmr,rgd|
|Link:||<Go to ISI>://A1996UL38200001|
|Appears in Collections:||Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)|
Files in This Item:
|Tsikaris-1996-Isomerization of the.pdf||723.28 kB||Adobe PDF||View/Open Request a copy|
Please use this identifier to cite or link to this item:This item is a favorite for 0 people.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.