Inhibition of human beta-tryptase by Bowman-Birk inhibitor derived peptides.
Four 11-residue peptides based on the Bowman-Birk inhibitor (BBI) structure were synthesized. These were tested for their ability to inhibit human beta-tryptase. Peptides with a basic residue at P1 inhibited tryptase even though the intact BBI protein is inactive. This result is interpreted in terms of the unique structural arrangement of active sites in tryptase which prevent access by large protein inhibitors.
Scarpi
D
D
Department of Chemistry, Imperial College of Science, Technology and Medicine, South Kensington, London, UK.
McBride
J D
JD
Leatherbarrow
R J
RJ
D006801:Humans; D009842:Oligopeptides / Q000138:chemical synthesis / Q000494:pharmacology*; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D014357:Trypsin / Q000378:metabolism; D053802:Tryptases
D009842:Oligopeptides; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; D014357:Trypsin; D053802:Tryptases