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Title: Chebulin: Terminalia chebula Retz. fruit-derived peptide with angiotensin-I-converting enzyme inhibitory activity
Authors: Thakorn Sornwatana
Kunan Bangphoomi
Sittiruk Roytrakul
Nuanchawee Wetprasit
Kiattawee Choowongkomon
Sunanta Ratanapo
Kasetsart University
Mahidol University
Thailand National Center for Genetic Engineering and Biotechnology
Ramkhamhaeng University
Keywords: Biochemistry, Genetics and Molecular Biology;Chemical Engineering;Engineering;Immunology and Microbiology
Issue Date: 1-Nov-2015
Citation: Biotechnology and Applied Biochemistry. Vol.62, No.6 (2015), 746-753
Abstract: © 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.
ISSN: 14708744
Appears in Collections:Scopus 2011-2015

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