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Purpose <p>Goat whey protein (GWP) is recognized as a valuable source of bioactive peptides with significant health-promoting properties. This study aimed to generate, identify, and characterise bioactive peptides from enzymatically hydrolysed GWP and to analyse their binding interactions with key metabolic enzymes involved in lipid and carbohydate digestion. </p> Methods <p> GWP was enzymatically hydrolyzed using a combination of gastrointestinal enzymes pepsin, trypsin, and chymotrypsin to simulate physiological digestion and release bioactive peptides. The resulting peptides were identified through high-resolution liquid chromatography-mass spectrometry (HR-LC/MS). Bioactivity prediction was performed using PeptideRanker, and toxicity was assessed in in silico. Molecular docking simulations were conducted to evaluate peptide interactions with pancreatic lipase and alpha-amylase, two critical enzymes in fat and carbohydrate metabolism. </p> Results <p>Mass spectrometry analysis resulting in library of 2883 peptides with lengths ranging from 6 to 44 amino acids. Among them, 40 peptides were predicted to exhibit high bioactivity scores (0.90–1), with 28 of these being classified as nontoxic. Molecular docking analysis demonstrated strong binding interactions between the selected peptides and the target metabolic enzymes. Notably, WPGIMR and WQDGSWQF exhibited the highest binding affinities toward pancreatic lipase, whereas AAPFIWL showed significant interaction with α-amylase. Importantly, WQDGSWQF displayed dual inhibitory potential, forming interactions with both pancreatic lipase and α-amylase. These results underscore the promising multi-target inhibitory capacity of the identified peptides against key enzymes implicated in obesity and type 2 diabetes.</p> Conclusion <p> This study shed light on the molecular mechanisms underlying the inhibitory activities of whey protein-derived peptides. They highlight their potential applications as functional food ingredients or natural therapeutic agents for managing metabolic disorders such as obesity and diabetes, advancing the understanding of whey protein hydrolysates in modulating key metabolic enzymes.</p>

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Mass Spectrometry-Guided Library Preparation of Peptides as Metabolic Enzyme Natural Inhibitors for the Management of Obesity and Diabetes

  • 期刊论文

  • 发表日期：

    2026年2月26日

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  • Manish Singh Sansi,
  • Daraksha Iram,
  • Sunny Kalyan,
  • Sudarshan Kumar,
  • Suman Kapila,
  • Kamal Gandhi,
  • Sunita Meena

摘要

Purpose

Goat whey protein (GWP) is recognized as a valuable source of bioactive peptides with significant health-promoting properties. This study aimed to generate, identify, and characterise bioactive peptides from enzymatically hydrolysed GWP and to analyse their binding interactions with key metabolic enzymes involved in lipid and carbohydate digestion.

Methods

GWP was enzymatically hydrolyzed using a combination of gastrointestinal enzymes pepsin, trypsin, and chymotrypsin to simulate physiological digestion and release bioactive peptides. The resulting peptides were identified through high-resolution liquid chromatography-mass spectrometry (HR-LC/MS). Bioactivity prediction was performed using PeptideRanker, and toxicity was assessed in in silico. Molecular docking simulations were conducted to evaluate peptide interactions with pancreatic lipase and alpha-amylase, two critical enzymes in fat and carbohydrate metabolism.

Results

Mass spectrometry analysis resulting in library of 2883 peptides with lengths ranging from 6 to 44 amino acids. Among them, 40 peptides were predicted to exhibit high bioactivity scores (0.90–1), with 28 of these being classified as nontoxic. Molecular docking analysis demonstrated strong binding interactions between the selected peptides and the target metabolic enzymes. Notably, WPGIMR and WQDGSWQF exhibited the highest binding affinities toward pancreatic lipase, whereas AAPFIWL showed significant interaction with α-amylase. Importantly, WQDGSWQF displayed dual inhibitory potential, forming interactions with both pancreatic lipase and α-amylase. These results underscore the promising multi-target inhibitory capacity of the identified peptides against key enzymes implicated in obesity and type 2 diabetes.

Conclusion

This study shed light on the molecular mechanisms underlying the inhibitory activities of whey protein-derived peptides. They highlight their potential applications as functional food ingredients or natural therapeutic agents for managing metabolic disorders such as obesity and diabetes, advancing the understanding of whey protein hydrolysates in modulating key metabolic enzymes.