Conformational study of linear and cyclic peptides corresponding to the 276-284 epitope region of HSV gD-1

G. Mező, Zs. Majer, E. Vass, M. A. Jimenez, D. Andreu, F. Hudecz

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The results of conformational analysis of linear and cyclic peptides from the 276SALLEDPVG284 sequence of glycoprotein D of Herpes simplex virus are presented. The epitope peptides were synthesized by SPPS and on resin cyclization was applied for preparation of cyclic compounds. Circular dichroism spectroscopy, Fourier-transform infrared spectroscopy and nuclear magnetic resonance (NMR) were used to determine of the solution structure of both linear and cyclic peptides. The results indicated that the cyclopeptides containing the core of the epitope (DPVG) as a part of the cycle have more stable β-turn structure than the linear peptides or the cyclic analogues, where the core motif is not a part of the cycle. NMR study of H-SALLc(EDPVGK)-NH2 confirm presence of a type I β-turn structure which includes the DPVG epitope core.

Original languageEnglish
Pages (from-to)51-65
Number of pages15
JournalBiophysical Chemistry
Volume103
Issue number1
DOIs
Publication statusPublished - Jan 8 2003

Fingerprint

Cyclic Peptides
Human Herpesvirus 1
peptides
Epitopes
Nuclear magnetic resonance
Circular dichroism spectroscopy
Peptides
Magnetic Resonance Spectroscopy
Cyclization
cyclic compounds
Viruses
nuclear magnetic resonance
cycles
Glycoproteins
viruses
Fourier Transform Infrared Spectroscopy
Simplexvirus
Resins
Circular Dichroism
resins

Keywords

  • Conformation of cyclic peptides
  • Cyclic epitope peptides
  • HSV gD-1
  • On resin peptide cyclization

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Biophysics

Cite this

Conformational study of linear and cyclic peptides corresponding to the 276-284 epitope region of HSV gD-1. / Mező, G.; Majer, Zs.; Vass, E.; Jimenez, M. A.; Andreu, D.; Hudecz, F.

In: Biophysical Chemistry, Vol. 103, No. 1, 08.01.2003, p. 51-65.

Research output: Contribution to journalArticle

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AU - Mező, G.

AU - Majer, Zs.

AU - Vass, E.

AU - Jimenez, M. A.

AU - Andreu, D.

AU - Hudecz, F.

PY - 2003/1/8

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N2 - The results of conformational analysis of linear and cyclic peptides from the 276SALLEDPVG284 sequence of glycoprotein D of Herpes simplex virus are presented. The epitope peptides were synthesized by SPPS and on resin cyclization was applied for preparation of cyclic compounds. Circular dichroism spectroscopy, Fourier-transform infrared spectroscopy and nuclear magnetic resonance (NMR) were used to determine of the solution structure of both linear and cyclic peptides. The results indicated that the cyclopeptides containing the core of the epitope (DPVG) as a part of the cycle have more stable β-turn structure than the linear peptides or the cyclic analogues, where the core motif is not a part of the cycle. NMR study of H-SALLc(EDPVGK)-NH2 confirm presence of a type I β-turn structure which includes the DPVG epitope core.

AB - The results of conformational analysis of linear and cyclic peptides from the 276SALLEDPVG284 sequence of glycoprotein D of Herpes simplex virus are presented. The epitope peptides were synthesized by SPPS and on resin cyclization was applied for preparation of cyclic compounds. Circular dichroism spectroscopy, Fourier-transform infrared spectroscopy and nuclear magnetic resonance (NMR) were used to determine of the solution structure of both linear and cyclic peptides. The results indicated that the cyclopeptides containing the core of the epitope (DPVG) as a part of the cycle have more stable β-turn structure than the linear peptides or the cyclic analogues, where the core motif is not a part of the cycle. NMR study of H-SALLc(EDPVGK)-NH2 confirm presence of a type I β-turn structure which includes the DPVG epitope core.

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KW - Cyclic epitope peptides

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KW - On resin peptide cyclization

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