A new helicoid-type sequential oligopeptide carrier (SOCn) for developing potent antigens and immunogens

Sakarellos-Daitsiotis, M; Tsikaris, V; Sakarellos, C; Vlachoyiannopoulos, PG; Tzioufas, AG; Moutsopoulos, HH

dc.contributor.author	Sakarellos-Daitsiotis, M	en
dc.contributor.author	Tsikaris, V	en
dc.contributor.author	Sakarellos, C	en
dc.contributor.author	Vlachoyiannopoulos, PG	en
dc.contributor.author	Tzioufas, AG	en
dc.contributor.author	Moutsopoulos, HH	en
dc.date.accessioned	2014-03-01T01:48:49Z
dc.date.available	2014-03-01T01:48:49Z
dc.date.issued	1999	en
dc.identifier.issn	0264-410X	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/25604
dc.subject	peptide carriers	en
dc.subject	carriers of immunogenic peptides	en
dc.subject	vaccines	en
dc.subject	synthesis of carriers	en
dc.subject	peptide conformation	en
dc.subject	H-1-NMR spectroscopy	en
dc.subject	immunoassays	en
dc.subject	immune response	en
dc.subject	autoimmune diseases	en
dc.subject.classification	Immunology	en
dc.subject.classification	Medicine, Research & Experimental	en
dc.subject.classification	Veterinary Sciences	en
dc.subject.other	T-CELL	en
dc.subject.other	SYNTHETIC PEPTIDES	en
dc.subject.other	REPETITIVE EPITOPE	en
dc.subject.other	SM AUTOANTIGEN	en
dc.subject.other	SPECIFICITY	en
dc.subject.other	AUTOANTIBODIES	en
dc.subject.other	ANTIBODIES	en
dc.subject.other	DESIGN	en
dc.subject.other	VACCINES	en
dc.subject.other	LA/SSB	en
dc.title	A new helicoid-type sequential oligopeptide carrier (SOCn) for developing potent antigens and immunogens	en
heal.type	journalArticle	en
heal.language	English	en
heal.publicationDate	1999	en
heal.abstract	A new class of sequential oligopeptide carriers (SOCn) for anchoring antigenic/immunogenic peptides has been constructed. The carrier, formed by the repetitive Lys-Aib-Gly moiety, is designed to display a predetermined 3D structure, so that the attached peptides would obtain a defined spatial orientation. Conformational analysis showed that SOCn, adopt a distorted 3(10)-helical structure, while the coupled peptides preserve their original 'active' structure. Coupling to the carrier may also result to the enhancement of one conformer of the anchored peptide. Tt is concluded that the structure of SOCn offers an optimal presentation of the attached peptides, so that potent antigens or immunogens are generated. (C) 1999 Elsevier Science Ltd. All rights reserved.	en
heal.publisher	ELSEVIER SCI LTD	en
heal.journalName	VACCINE	en
dc.identifier.isi	ISI:000083201100014	en
dc.identifier.volume	18	en
dc.identifier.issue	3-4	en
dc.identifier.spage	302	en
dc.identifier.epage	310	en