The effect of cyclization on the enzymatic degradation of herpes simplex virus glycoprotein D derived epitope peptide

Regina Tugyi, G. Mező, Erzsébet Fellinger, David Andreu, F. Hudecz

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

One linear and three cyclic peptides corresponding to the 278-287 (278LLEDPVGTVA287) sequence of glycoprotein D (gD-1) of herpes simplex virus were synthesized for the analysis of the effect of cyclization on protection against enzymatic degradation. In this design, the turn-forming motif (281DPVG284) was positioned in the central part of the peptide and elongated by three amino acids at both termini. Cyclopeptide formation was achieved by the introduction of a peptide bond, a disulfide bridge or a thioether link. The stability of these peptides was compared in human serum and also in rat lysosomal preparations. The data obtained in 10% and 50% human serum show that all three types of cyclization enhanced the stability, but at different levels. Complete stability was only achieved by the introduction of a thioether link, while the presence of a disulfide or peptide bond resulted in improved, but partial resistance against hydrolytic decomposition. In lysosomal preparations the presence of cyclic primary structure provided full protection against enzymatic hydrolysis. Taken together, these findings indicate that by appropriate structural modification it is feasible to construct a synthetic antigen with high stability against enzymatic degradation in complex biological fluids. Further studies are in progress to identify enzymes responsible for degradation in diluted human sera as well as in the lysosomal preparations and to gain more detailed information on the mechanism of action.

Original languageEnglish
Pages (from-to)642-649
Number of pages8
JournalJournal of Peptide Science
Volume11
Issue number10
DOIs
Publication statusPublished - Oct 2005

Fingerprint

Cyclization
Simplexvirus
Viruses
Epitopes
Glycoproteins
Degradation
Cyclic Peptides
Peptides
Sulfides
Disulfides
Serum
Synthetic Vaccines
Enzymatic hydrolysis
Rats
Hydrolysis
Decomposition
Amino Acids
Fluids
Enzymes

Keywords

  • Cyclopeptides
  • Epitope
  • HSV gD-1
  • Human serum
  • Lysosomal degradation
  • Proteolytic stability

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

The effect of cyclization on the enzymatic degradation of herpes simplex virus glycoprotein D derived epitope peptide. / Tugyi, Regina; Mező, G.; Fellinger, Erzsébet; Andreu, David; Hudecz, F.

In: Journal of Peptide Science, Vol. 11, No. 10, 10.2005, p. 642-649.

Research output: Contribution to journalArticle

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