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Purpose <p>This study provides the first systematic identification of antidiabetic peptides from Bikaneri camel milk (Indian camel breed), a genetic resource that has not been investigated previously despite longstanding evidence of its metabolic benefits.</p> Methods <p>Casein and whey proteins were hydrolyzed using gastrointestinal proteases—pepsin (P), trypsin (T), and chymotrypsin (C)—singly and sequentially to mimic physiological digestion; hydrolysates were enriched via ≤3 kDa ultrafiltration, a dual strategy enhancing gastrointestinal stability and selectively exposing low-molecular-weight peptides with superior bioactivity. GLP-1 secretagogue activity and DPP-IV inhibition were evaluated. Peptide identification was performed using LC–MS/MS, followed by bioactivity prediction, molecular docking, ADMET analysis, and network pharmacology.</p> Results <p>Among fourteen hydrolysates, the ≤3 kDa fractions of H<sub>PC</sub> (Bikaneri camel milk casein hydrolysates; BCMCHs) and H<sub>PTC</sub> (Bikaneri camel whey protein hydrolysates; BCMWPHs) showed the strongest GLP-1 secretagogue (2.695 ± 0.056 and 2.814 ± 0.124 ng/mL) and DPP-IV inhibitory (66.55 ± 0.58% and 77.87 ± 1.15%) activities . LC–MS/MS identified over ~4000 peptides, from which eight were shortlisted based on bioactivity prediction scores, significant DPP-IV binding potential, key structural motifs, and in vitro characterization. Among them, NWYYPPQ (NQ-7) and TAGWNIPMGL (TL-10) exhibited strong dual activity, with GLP-1 secretion of 3.59 ± 0.56 and 3.64 ± 0.47 ng/mL and DPP-IV inhibition (IC₅₀: 55.51 ± 6.4; 118.0 ± 2.07 μM), acting through non-competitive and competitive modes, respectively. Molecular docking confirmed that both peptides interact with DPP-IV via hydrogen bonds, electrostatic, and hydrophobic interactions. ADMET predictions indicated favourable distribution, metabolic stability, and safety. Network pharmacology further suggested roles in calcium signaling, apoptosis, nitrogen metabolism, and chemokine regulation.</p> Conclusion <p>Overall, this study provides the first peptide-level evidence that Bikaneri camel milk contains novel GLP-1–stimulating and DPP-IV–inhibitory peptides, highlighting its antidiabetic potential.</p>

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Bikaneri Camel Milk-Derived Low-Molecular-Weight Peptides as a Novel Therapeutic Approach for Diabetes

  • 期刊论文

  • 发表日期：

    2026年3月7日

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  • Sunny Kalyan,
  • Rakesh Kumar Raman,
  • Dipanjan Misra,
  • Manish Singh Sansi,
  • Sunita Meena

摘要

Purpose

This study provides the first systematic identification of antidiabetic peptides from Bikaneri camel milk (Indian camel breed), a genetic resource that has not been investigated previously despite longstanding evidence of its metabolic benefits.

Methods

Casein and whey proteins were hydrolyzed using gastrointestinal proteases—pepsin (P), trypsin (T), and chymotrypsin (C)—singly and sequentially to mimic physiological digestion; hydrolysates were enriched via ≤3 kDa ultrafiltration, a dual strategy enhancing gastrointestinal stability and selectively exposing low-molecular-weight peptides with superior bioactivity. GLP-1 secretagogue activity and DPP-IV inhibition were evaluated. Peptide identification was performed using LC–MS/MS, followed by bioactivity prediction, molecular docking, ADMET analysis, and network pharmacology.

Results

Among fourteen hydrolysates, the ≤3 kDa fractions of HPC (Bikaneri camel milk casein hydrolysates; BCMCHs) and HPTC (Bikaneri camel whey protein hydrolysates; BCMWPHs) showed the strongest GLP-1 secretagogue (2.695 ± 0.056 and 2.814 ± 0.124 ng/mL) and DPP-IV inhibitory (66.55 ± 0.58% and 77.87 ± 1.15%) activities . LC–MS/MS identified over ~4000 peptides, from which eight were shortlisted based on bioactivity prediction scores, significant DPP-IV binding potential, key structural motifs, and in vitro characterization. Among them, NWYYPPQ (NQ-7) and TAGWNIPMGL (TL-10) exhibited strong dual activity, with GLP-1 secretion of 3.59 ± 0.56 and 3.64 ± 0.47 ng/mL and DPP-IV inhibition (IC₅₀: 55.51 ± 6.4; 118.0 ± 2.07 μM), acting through non-competitive and competitive modes, respectively. Molecular docking confirmed that both peptides interact with DPP-IV via hydrogen bonds, electrostatic, and hydrophobic interactions. ADMET predictions indicated favourable distribution, metabolic stability, and safety. Network pharmacology further suggested roles in calcium signaling, apoptosis, nitrogen metabolism, and chemokine regulation.

Conclusion

Overall, this study provides the first peptide-level evidence that Bikaneri camel milk contains novel GLP-1–stimulating and DPP-IV–inhibitory peptides, highlighting its antidiabetic potential.