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Influence of sequential oligopeptide carriers on the bioactive structure of conjugated epitopes: Comparative study of the conformation of a Herpes simplex virus glycoprotein gD‐1 epitope in the free and conjugated form, and protein “built‐in” crystal structure

Influence of sequential oligopeptide carriers on the bioactive structure of conjugated epitopes:... Synthetic carriers play an important role in immunogen presentation, due to their ability of inducing improved and specific responses to conjugated epitopes. Their influence on the bioactive conformation of the epitope, though admittedly crucial for relevant in vitro and in vivo applications, is difficult to evaluate, given the usual lack of information on the complex conformational features determined by the nature of the carrier and the mode of ligation. Using the Herpes simplex virus glycoprotein D‐1 epitope (Leu9–Lys–Nle–Ala–Asp–Pro–Asn–Arg–Phe–Arg–Gly–Lys–Asp–Leu22) as a model, we have performed a detailed conformational analysis on the free epitope peptide in solution and on three constructs in which the epitope was conjugated to sequential oligopeptide carriers {Ac–(Lys–Aib–Gly)4–OH (SOC4)} (through either a thioether or an amide bond; Ac: acetyl) and polytuftsin oligomers {H–(Thr–Lys–Pro–Lys–Gly)4–NH2 (T20)}, (through a thioether bond). The analysis of the epitope conformation in the parent protein, in carrier‐conjugated and free form, suggests that the β‐turn structure of the –Asp13–Pro–Asn–Arg16– segment is highly conserved and independent of the epitope form. However, small conformational variations were observed at the C‐terminal part of the epitope, depending on the nature of the carrier. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 383–399, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biopolymers Wiley

Influence of sequential oligopeptide carriers on the bioactive structure of conjugated epitopes: Comparative study of the conformation of a Herpes simplex virus glycoprotein gD‐1 epitope in the free and conjugated form, and protein “built‐in” crystal structure

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References (46)

Publisher
Wiley
Copyright
Copyright © 2006 Wiley Periodicals, Inc., A Wiley Company
ISSN
0006-3525
eISSN
1097-0282
DOI
10.1002/bip.20486
pmid
16493659
Publisher site
See Article on Publisher Site

Abstract

Synthetic carriers play an important role in immunogen presentation, due to their ability of inducing improved and specific responses to conjugated epitopes. Their influence on the bioactive conformation of the epitope, though admittedly crucial for relevant in vitro and in vivo applications, is difficult to evaluate, given the usual lack of information on the complex conformational features determined by the nature of the carrier and the mode of ligation. Using the Herpes simplex virus glycoprotein D‐1 epitope (Leu9–Lys–Nle–Ala–Asp–Pro–Asn–Arg–Phe–Arg–Gly–Lys–Asp–Leu22) as a model, we have performed a detailed conformational analysis on the free epitope peptide in solution and on three constructs in which the epitope was conjugated to sequential oligopeptide carriers {Ac–(Lys–Aib–Gly)4–OH (SOC4)} (through either a thioether or an amide bond; Ac: acetyl) and polytuftsin oligomers {H–(Thr–Lys–Pro–Lys–Gly)4–NH2 (T20)}, (through a thioether bond). The analysis of the epitope conformation in the parent protein, in carrier‐conjugated and free form, suggests that the β‐turn structure of the –Asp13–Pro–Asn–Arg16– segment is highly conserved and independent of the epitope form. However, small conformational variations were observed at the C‐terminal part of the epitope, depending on the nature of the carrier. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 383–399, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

Journal

Biopolymers – Wiley

Published: Jan 1, 2006

Keywords: conformation of conjugated epitope peptides; glycoprotein D‐1 epitope; sequential oligopeptide carriers; sequential oligopeptide carriers; tetratuftsin carrier; synthetic carriers; carrier‐conjugated epitopes

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