Studies on the Active Site and Antihypertensive Activity of Angiotensin I-Converting Enzyme Inhibitors Derived from Casein

摘要: The fragment-peptides of angiotensin I-converting enzyme inhibitors (CEI12, CEI5 and CEIβ7) derived from an enzymatic hydrolysate casein were synthesized. Val-Ala-Pro, the C-terminal tripeptide (Phe-Phe-Val-Ala-Pro), exhibited more potent inhibitory activity (I50 = 2.0μm) than 6.0μm). However, d-Val-Ala-Pro showed lower 550μm). Val-Ala-Pro may be important for CEI5. heptapeptide CEI12 (Phe-Phe-Val-Ala-Pro-Phe-Pro-Glu-Val-Phe-Gly-Lys) short fragments CEIβ7 (Ala-Val-Pro-Tyr-Pro-Gln-Arg) activities full-length peptides.Also, antihypertensive was investigated. CEI12, intravenously administered to anesthetized rats at 14.2 mg/kg, antagonized rats’ pressor response I.