# Peptides from ‘Vaina Morada’ Black Bean Inhibit α-Amylase and α-Glucosidase: A Combined In Silico–In Vitro Study

**Authors:** Filiberto Ramirez-Lozano, Jonhatan Contreras, Arturo Alfaro-Diaz, Diego Armando Luna-Vital, Anne C. Gschaedler Mathis, Judith Esmeralda Urías-Silvas, Luis Mojica

PMC · DOI: 10.3390/foods14223847 · 2025-11-11

## TL;DR

This study shows that peptides from 'vaina morada' black beans can inhibit enzymes linked to diabetes, suggesting their potential use in functional foods.

## Contribution

The study identifies specific bioactive peptides from black beans with strong enzyme inhibition and antioxidant properties.

## Key findings

- Peptides from black bean hydrolysates inhibited α-amylase and α-glucosidase with IC50 values of 0.78 mg/mL and 0.60 mg/mL, respectively.
- Sequence VNDNGEPTL showed strong binding affinities of −10.0 kcal/mol and −11.8 kcal/mol for α-amylase and α-glucosidase, respectively.
- Dialyzed hydrolysates had the highest antioxidant activity with an IC25 of 38.83 µM TE/mg for DPPH.

## Abstract

The objective of this work was to evaluate the antidiabetes potential of protein hydrolysates derived from “vaina morada” black bean (Phaseolus vulgaris L.). Bioactive peptide sequences were identified after in silico digestion. The biological activities and molecular interactions of peptides with targeted enzymes were assayed. The degree of hydrolysis and protein profile were evaluated throughout the processing stages, including protein extraction, hydrolysis, and dialysis. Biological potential assays, including antioxidant potential (DPPH and ABTS•+), and inhibition of α-amylase and α-glucosidase enzymes, were performed. Identified bioactive peptides showed potential for inhibiting ACE and DPP-IV, as well as exhibiting antioxidant potential. Molecular docking indicated that several peptide sequences showed equal or stronger binding affinities compared to acarbose. Notably, sequence VNDNGEPTL exhibited binding energies of −10.0 kcal/mol (α-amylase) and −11.8 kcal/mol (α-glucosidase). Protein hydrolysates showed the lowest IC50 (113.16 µM TE/mg for ABTS•+), while dialyzed protein hydrolysates demonstrated the strongest activity for DPPH (IC25 of 38.83 µM TE/mg). Also, the dialyzed hydrolysate demonstrated the highest enzyme inhibition, with IC50 values of 0.78 mg/mL for α-amylase and 0.60 mg/mL for α-glucosidase. “Vaina morada” black bean protein hydrolysates are a rich source of multifunctional peptides, supporting their potential application in functional food formulations aimed at preventing or managing type 2 diabetes.

## Linked entities

- **Proteins:** ACE (angiotensin I converting enzyme), DPP4 (dipeptidyl peptidase 4)
- **Chemicals:** acarbose (PubChem CID 9811704), ABTS•+ (PubChem CID 35688)
- **Diseases:** type 2 diabetes (MONDO:0005148)

## Full-text entities

- **Diseases:** type 2 diabetes (MESH:D003924)
- **Chemicals:** 'Vaina Morada' Black Bean (-), acarbose (MESH:D020909), DPPH (MESH:C004931), ABTS + (MESH:C002502)
- **Species:** Phaseolus vulgaris (common bean, species) [taxon 3885]

## Figures

6 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12651079/full.md

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Source: https://tomesphere.com/paper/PMC12651079