Engineering new peptidic inhibitors from a natural chymotrypsin inhibitor

Zoltán Mucsi, A. Perczel, G. Orosz

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Three model peptides of different sizes (17-24 amino acid residues), mimicking the chymotrypsin inhibitor SCGI (a peptide of 35 amino acid residues) isolated from Schistocerca gregaria were designed and prepared by convergent peptide synthesis. Selective formation of disulphide bridges in the closing step was achieved without selective protection of cysteine residues. The natural pattern of the two disulphide bridges was determined by 2D homonuclear 1H NMR techniques. All three model peptides were characterized by amino acid analysis, MS and CD spectra. Preliminary results revealed that the two smaller model peptides exhibit no inhibitory activity, whereas the larger one shows limited inhibition of chymotrypsin.

Original languageEnglish
Pages (from-to)643-655
Number of pages13
JournalJournal of Peptide Science
Volume8
Issue number12
DOIs
Publication statusPublished - Dec 1 2002

Fingerprint

Chymotrypsin
Peptides
Amino Acids
Disulfides
Plant shutdowns
Cysteine
Nuclear magnetic resonance

Keywords

  • Chymotrypsin inhibitor
  • Convergent peptide synthesis
  • Molecular modelling
  • Peptide design
  • Selective disulphide bridge formation

ASJC Scopus subject areas

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

Cite this

Engineering new peptidic inhibitors from a natural chymotrypsin inhibitor. / Mucsi, Zoltán; Perczel, A.; Orosz, G.

In: Journal of Peptide Science, Vol. 8, No. 12, 01.12.2002, p. 643-655.

Research output: Contribution to journalArticle

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