Conformational study of the complementary peptide to a B-cell epitope of the La/SSB autoantigen

Hemmerlin, C; Du, APC; Elhilali, Z; Moulia, A; Tsikaris, V; Sakarellos-Daitsiotis, M; Sakarellos, C; Dotsika, E; Tzioufas, AG; Moutsopoulos, HM; Cung, MT

dc.contributor.author	Hemmerlin, C	en
dc.contributor.author	Du, APC	en
dc.contributor.author	Elhilali, Z	en
dc.contributor.author	Moulia, A	en
dc.contributor.author	Tsikaris, V	en
dc.contributor.author	Sakarellos-Daitsiotis, M	en
dc.contributor.author	Sakarellos, C	en
dc.contributor.author	Dotsika, E	en
dc.contributor.author	Tzioufas, AG	en
dc.contributor.author	Moutsopoulos, HM	en
dc.contributor.author	Cung, MT	en
dc.date.accessioned	2014-03-01T01:51:02Z
dc.date.available	2014-03-01T01:51:02Z
dc.date.issued	2001	en
dc.identifier.issn	1387-1609	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/26226
dc.subject	Sjogren's syndrome	en
dc.subject	2D-NMR	en
dc.subject	NOESY	en
dc.subject	molecular modelling	en
dc.subject	complementary peptide	en
dc.subject	antigenic peptide	en
dc.subject.classification	Chemistry, Multidisciplinary	en
dc.subject.other	SPECIFICITY	en
dc.subject.other	AUTOANTIBODIES	en
dc.title	Conformational study of the complementary peptide to a B-cell epitope of the La/SSB autoantigen	en
heal.type	journalArticle	en
heal.language	English	en
heal.publicationDate	2001	en
heal.abstract	Starting from the 20-mer peptide 289-308, one of the experimentally characterized B-cell epitopes of the La/SSB autoantigen, the complementary peptide cpl(289-308), encoded by the complementary RNA was designed. The conformational properties of the cpl(289-308) were investigated in DMSO solution with the combined use of NMR data (vicinal coupling constants, NOE effects and temperature coefficient values), molecular modelling calculations of energy minimization and molecular dynamics. MD calculations led to a folded structure in which a betaI-turn, stabilized by the H-8 amide proton to the F-5 carbonyl hydrogen bond, was found for the F5P6S7H8 sequence, whereas two gamma -turns, centred around the E-15 and I-18 residues respectively, were found in the C-terminal part of the peptide. In the whole crown folded structure of the peptide, the Y-4, F-5, H-8, F-9 and F-10 aromatic side chains are situated on one side with the E-13, E-15, T-17 and Cc side chains on the other. This 3D structure resembles and could mimic the binding site of an antibody. (C) 2001 Academic des sciences/Editions scientifiques et medicales Elsevier SAS.	en
heal.publisher	EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER	en
heal.journalName	COMPTES RENDUS DE L ACADEMIE DES SCIENCES SERIE II FASCICULE C-CHIMIE	en
dc.identifier.isi	ISI:000172445600003	en
dc.identifier.volume	4	en
dc.identifier.issue	10	en
dc.identifier.spage	729	en
dc.identifier.epage	733	en