Thakorn SornwatanaKunan BangphoomiSittiruk RoytrakulNuanchawee WetprasitKiattawee ChoowongkomonSunanta RatanapoKasetsart UniversityMahidol UniversityThailand National Center for Genetic Engineering and BiotechnologyRamkhamhaeng University2018-11-232018-11-232015-11-01Biotechnology and Applied Biochemistry. Vol.62, No.6 (2015), 746-75314708744088545132-s2.0-84955186378https://repository.li.mahidol.ac.th/handle/123456789/35356© 2014 International Union of Biochemistry and Molecular Biology, Inc. Angiotensin-I-converting enzyme (ACE) plays an important role in blood pressure regulation. In this study, an ACE-hexapeptide inhibitor (Asp-Glu-Asn-Ser-Lys-Phe) designated as chebulin was produced from the fruit protein of Terminalia chebula Retz. by pepsin digestion, ultrafiltrated through a 3 KDa cut-off membrane, a reverse-phase high-performance liquid chromatography, and nano-liquid chromatography tandem mass spectrometry analysis. Chebulin was found to inhibit ACE in a noncompetitive manner, as supported by the structural model. It bounds to ACE by the hydrogen bond, hydrophobic and ionic interactions via the interactions of C-terminal Phe (Phe-6), and N-terminal residues (Asp-1 and Glu-2) with the amino acid residues on noncatalytic sites of the ACE. The results showed that chebulin derived from fruits of T. chebula Retz. is a potential ACE-peptide inhibitor that could be used as a functional food additive for the prevention of hypertension and as an alternative to ACE inhibitor drug.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyChemical EngineeringEngineeringImmunology and MicrobiologyArticleSCOPUS10.1002/bab.1321