title: Improvement of lipoxygenase inhibition by octapeptides.
abstract: The beta-casein-derived octapeptide RINKKIEK is a noncompetitive inhibitor of soybean lipoxygenase (LOX). To investigate the molecular determinants for the enzyme-peptide interaction, a peptide library containing substitutional analogs of RINKKIEK was prepared by SPOT synthesis and analyzed for interaction with fluorescent-labeled LOX. The positively charged amino acid residues in RINKKIEK appear to be essential for the LOX-peptide interaction. Replacement of the negatively charged glutamic acid by any other amino acid residue improves LOX binding. For both RINKKIPK and RINKKISK this increase in LOX binding is accompanied by a threefold increase in LOX inhibition.
authors.affiliation: Laboratory of Biochemistry, Wageningen University, P.O. Box 9101, 6700 HB Wageningen, The Netherlands. marloes.schurink@wur.nl
authors.forename: Marloes
authors.initials: M
authors.lastname: Schurink
authors.forename: Willem J H
authors.initials: WJ
authors.lastname: van Berkel
authors.forename: Harry J
authors.initials: HJ
authors.lastname: Wichers
authors.forename: Carmen G
authors.initials: CG
authors.lastname: Boeriu
mesh_terms: D019943:Amino Acid Substitution; D000818:Animals; D001093:Arachidonate 15-Lipoxygenase / Q000378:metabolism; D005456:Fluorescent Dyes; D007700:Kinetics; D008084:Lipoxygenase / Q000187:drug effects / Q000378:metabolism; D016859:Lipoxygenase Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D009842:Oligopeptides / Q000737:chemistry* / Q000494:pharmacology*; D019151:Peptide Library; D011817:Rabbits; D013025:Glycine max / Q000201:enzymology; D013050:Spectrometry, Fluorescence
chemical_list: D005456:Fluorescent Dyes; D016859:Lipoxygenase Inhibitors; D009842:Oligopeptides; D019151:Peptide Library; C101084:lipoxygenase L-1; D008084:Lipoxygenase; D001093:Arachidonate 15-Lipoxygenase