Chebulin: Terminalia chebula Retz. fruit‐derived peptide with angiotensin‐I–converting enzyme inhibitory activity

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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.
Funding Information
  • Kasetsart University Research and Development Institute

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