Engineering new peptidic inhibitors from a natural chymotrypsin inhibitor

Authors

  • Zoltán Mucsi,

    1. Department of Organic Chemistry, Eötvös Loránd University, Budapest
    2. Research Group of Peptide Chemistry at Eötvös Loránd University, Hungarian Academy of Sciences, Budapest 112, Po Box 32, H-1518, Hungary
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  • András Perczel,

    1. Department of Organic Chemistry, Eötvös Loránd University, Budapest
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  • Dr György Orosz

    Corresponding author
    1. Research Group of Peptide Chemistry at Eötvös Loránd University, Hungarian Academy of Sciences, Budapest 112, Po Box 32, H-1518, Hungary
    • Research Group of Peptide Chemistry at Eötvös Loránd University, Hungarian Academy of Sciences, Budapest, Hungary.
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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 Schistocercagregaria 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. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.

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