Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 59, Issue 20, Pages 11234-11237Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf202902r
Keywords
Angiotensin; ACE; inhibition; peptide; hypertensive
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A series of peptides, derived from an ACE inhibitory peptide (VTVNPYKWLP) found in our previous work, were synthesized. Their half maximal inhibition concentrations (IC50) for ACE inhibition have been determined. The effect of amino acid sequence on ACE inhibition was discussed on the basis of IC50 of the synthetic peptides, and the following characteristics of the ACE inhibitory peptide have been clarified. First, the active portion of this peptide for ACE inhibition is KW. Second, the amino acid sequences near this dipeptide (KW) have a strong effect on the inhibitory activity. Especially, the proline residue in the C-terminal end strongly enhanced ACE inhibition. It should be noted that the IC50 value of KWLP (5.5 mu M) is the same as the ACE inhibitory peptide (VTVNPYKWLP) and that the IC50 value of KW is 7.8 mu M. The stability and absorption efficiency in vivo would be significantly improved by shortening the peptide length from 10 amino acids to four amino acids or two amino acids.
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