Abstract
Abstract Peptides present in the repeating region in proline-rich proteins such a corn γ-zein, soybean cell wall protein (SbPRP1), carrot 33-kDa protein, collagen and mouse salivary gland protein were chemically synthesized. The prolyl endopeptidase (PEP, from Flavobacterium meningosepticum or bovine brain) inhibitory activity of these peptides was investigated. γ-Zein-related synthetic peptides such as His-Leu-Pro-Pro-Pro-Val and His-Leu-Pro-Pro-Pro-Val-His-Leu-Pro-Pro-Pro-Val inhibited PEP from both bacterial and mammalian sources. The IC 50 values of these peptides for F. meningosepticum PEP were 80 μM and 30 μM, respectively. Soybean cell wall protein-related synthetic peptides, Lys-Pro-Pro-Val and Lys-Pro-Pro-Ile also inhibited PEP to some degree. However, Pro-Pro-Pro-Pro-Gly-Gly-Pro-Gln-Pro-Arg-Pro-Pro-Glu-Gly (synthetic peptide fragment of salivary gland protein) and Gly-Pro-Hyp-Gly-Pro-Ala (fragment of collagen) showed hardly any inhibition. Therefore, we hydrolyzed γ-zein with subtilisin (Carlsberg) and confirmed the liberation of the native hexapeptide, His-Leu-Pro-Pro-Pro-Val.
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