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.
journal_name
Peptidesjournal_title
Peptidesauthors
Schurink M,van Berkel WJ,Wichers HJ,Boeriu CGdoi
10.1016/j.peptides.2007.09.018subject
Has Abstractpub_date
2007-12-01 00:00:00pages
2268-75issue
12eissn
0196-9781issn
1873-5169pii
S0196-9781(07)00395-6journal_volume
28pub_type
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