title: Chebulin: Terminalia chebula Retz. fruit-derived peptide with angiotensin-I-converting enzyme inhibitory activity.
abstract: 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.
authors.affiliation: Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok, Thailand.|Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand.
authors.forename: Thakorn
authors.initials: T
authors.lastname: Sornwatana
authors.affiliation: Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok, Thailand.
authors.forename: Kunan
authors.initials: K
authors.lastname: Bangphoomi
authors.affiliation: Genome Institute, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency (NSTDA), Klongluang, Pathumthani, Thailand.
authors.forename: Sittiruk
authors.initials: S
authors.lastname: Roytrakul
authors.affiliation: Department of Biotechnology, Faculty of Science, Ramkhamhaeng University, Bangkok, Thailand.
authors.forename: Nuanchawee
authors.initials: N
authors.lastname: Wetprasit
authors.affiliation: Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok, Thailand.
authors.forename: Kiattawee
authors.initials: K
authors.lastname: Choowongkomon
authors.affiliation: Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok, Thailand.
authors.forename: Sunanta
authors.initials: S
authors.lastname: Ratanapo
mesh_terms: D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D005638:Fruit / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism; D011487:Protein Conformation; D029766:Terminalia / Q000737:chemistry*
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides; D010940:Plant Proteins; D007703:Peptidyl-Dipeptidase A
keywords: Terminalia chebula; angiotensin-I-converting enzyme inhibition; chebulin; fruit protein; peptide