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Issue 5, 2015
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Peptides present in the non-digestible fraction of common beans (Phaseolus vulgaris L.) inhibit the angiotensin-I converting enzyme by interacting with its catalytic cavity independent of their antioxidant capacity

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Abstract

The aim was to evaluate the angiotensin-I converting enzyme (ACE) inhibitory potential and the antioxidant capacity of pure synthesized peptides (GLTSK, LSGNK, GEGSGA, MPACGSS and MTEEY) originally identified in the non-digestible fraction (NDF) of common beans (P. vulgaris L.) that had previously demonstrated antiproliferative activity against human colorectal cancer cells. The five peptides were able to inhibit ACE with half maximal inhibitory concentration (IC50) values ranging from 65.4 (GLTSK) to 191.5 μM (MPACGSS). The combination of GLTSK and MTEEY increased the ACE inhibition by 30% compared to equieffective doses of the single peptides. According to molecular docking analysis, the five peptides had lower estimated free energy values (−6.47 to −9.34 kcal mol−1) when they interacted with the catalytic site of ACE than that of the substrate hippuryl-histidyl-leucine (−5.41 kcal mol−1), thus inhibiting the enzymatic activity. According to molecular docking analysis, the five peptides interacted with four (His353, Ala354, Glu411 and Tyr523) out of 6 catalytic residues. Moreover, MPACGSS had the highest antioxidant activity according to Ferric reducing antioxidant power (FRAP) (421.58 μmol FeSO4 mg−1), Fe2+ chelation (2.01 μmol Na2EDTA mg−1) assays, and also in DPPH (748.39 μmol Trolox per mg of dry peptide) and ABTS (561.42 μmol Trolox mg−1) radical scavenging assays. The results support the hypothesis that peptides present in the non-digestible fraction of common beans (Phaseolus vulgaris L.) may exert their physiological benefits independent of their antioxidant capacity, by ACE inhibition through interaction with its catalytic cavity.

Graphical abstract: Peptides present in the non-digestible fraction of common beans (Phaseolus vulgaris L.) inhibit the angiotensin-I converting enzyme by interacting with its catalytic cavity independent of their antioxidant capacity

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Supplementary files

Article information


Submitted
24 Feb 2015
Accepted
26 Mar 2015
First published
27 Mar 2015

Food Funct., 2015,6, 1470-1479
Article type
Paper
Author version available

Peptides present in the non-digestible fraction of common beans (Phaseolus vulgaris L.) inhibit the angiotensin-I converting enzyme by interacting with its catalytic cavity independent of their antioxidant capacity

D. A. Luna-Vital, E. González de Mejía, S. Mendoza and G. Loarca-Piña, Food Funct., 2015, 6, 1470
DOI: 10.1039/C5FO00190K

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