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Peptides from Common Bean ( Phaseolus vulgaris L.) non‐Digestible Fraction Inhibit Angiotensin‐I Converting Enzyme by Interacting with Amino Acids in its Catalytic Cavity
Author(s) -
Luna Vital Diego,
Gonzalez de Mejia Elvira,
Mendoza Sandra,
LoarcaPina Guadalupe
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.924.17
Subject(s) - chemistry , trolox , antioxidant , abts , dpph , phaseolus , biochemistry , peptide , enzyme , food science , angiotensin converting enzyme , amino acid , botany , biology , endocrinology , blood pressure
Five major peptides (GLTSK, LGSNK, GEGSGA, MPACGSS and MTEEY) from non‐digestible fraction (NDF) of common bean have demonstrated antiproliferative activity against HCT116 and RKO human colorectal cancer cells. The aim was to evaluate angiotensin‐I converting enzyme (ACE) inhibitory activity and antioxidant capacity of peptides in common bean. For ACE inhibition, hippuril‐histidyl‐leucine was used as substrate and the product (hippuric acid) was quantified by HPLC. Antioxidant capacity was evaluated through FRAP, ABTS and DPPH assays. The inhibition of ACE ranged from IC 50 =33 to 91 µg of peptide/mL. Peptides inhibited ACE activity by interacting with residues His353, Ala354, Glu384, Glu411 and Tyr523 inside the catalytic cavity of the enzyme as determined by molecular docking. The peptide MPACGSS had the highest (p<0.05) antioxidant activity: 421.6 µmol FeSO4/mg (FRAP), 561.4 μmol Trolox/mg (ABTS) and 748.4 μmol Trolox/mg (DPPH). Since ACE inhibition and antioxidant activity may be involved in colorectal chemopreventive mechanisms, the results support the notion that peptides in common bean can contribute to colon health. Supported by University of Illinois and University of Queretaro research program