Skip to content
DraconiticResearch
Search Sources API
203,203 studies31 sourcesUpdated 48 min ago
Peer-reviewedCC BYFood Chemistry: X

Peptidomics-guided 3D structural-mechanistic investigation of bovine colostrum peptides reveals multi-targeted

  • Shashank M. Patil1
  • Ramith Ramu2
  • Kalirajan Rajagopal3
  • Vivek Hamse Kameshwar4
4 affiliations
  1. 1Department of Biotechnology & Bioinformatics, School of Life Sciences, JSS Academy of Higher Education & Research (JSS AHER), Mysuru 570015, Karnataka, India
  2. 2Department of Biotechnology & Bioinformatics, School of Life Sciences, JSS Academy of Higher Education & Research (JSS AHER), Mysuru 570015, Karnataka, India; Corresponding author.
  3. 3Department of Pharmaceutical Chemistry, JSS College of Pharmacy, JSS Academy of Higher Education & Research, Ooty, Nilgiris 643001, Tamil Nadu, India
  4. 4Department of Biotechnology, Adichunchanagiri School of Natural Sciences, Adichunchanagiri University, B.G. Nagara, Mandya, Karnataka 571448, India
Read full textDOICite

Abstract

Multi-target inhibition of α-amylase, α-glucosidase, and human aldose reductase can significantly address postprandial hyperglycemia and subsequent diabetic complications, yet bovine colostrum peptides remain largely unscreened against these enzymes. Using a peptidomics-guided, integrated in silico and in vitro approach, we identified three lead peptides and highlighted Peptide P2 (GPAGPQGPR) as a common lead inhibitor, showing favorable predicted binding and interaction profiles relative to the reference inhibitors. A dedicated 3D-structural analysis, including residue mapping, RMSF profiles, hydrophobicity surfaces, and intramolecular contact networks, suggested that the glycine-proline-rich scaffold of P2 may support predicted conformational adaptability and interactions with multiple enzyme targets. These findings were supported by in vitro enzyme inhibition and kinetic analyses, which indicated that P2 was consistent with a competitive inhibition model, while radical scavenging analysis indicated its antioxidant potential. These findings establish bovine colostrum as a potential multi-target antidiabetic and antioxidant peptide source, and present a structure-informed, reproducible framework for food-derived peptide discovery.

Related

  1. Structural basis for inhibition of the lipid flippase MurJ by phage lysis protein SglPP7 suggests convergent evolution with other Sgl peptides
    Kaito Hosoda, Hidetaka Kohga, Sixian Wu +5
    PLOS BiologyPeer-reviewedCC BY 4.0Full textMolecular biology & gene regulationBioinformatics & computational biologyPLOSPMC
  2. Prediction of Lindane-Induced Breast Cancer Toxicity Through Multi-Target Network Analysis and Mechanistic Investigation
    Yuze Lin, Jiahui Xu, Mingyang Sheng +5
    International Journal of Molecular SciencesPeer-reviewedCC BY 4.0Full textGeneral biochemistryCrossrefEurope PMC
  3. Structural and mechanistic divergence of the small (p)ppGpp synthetases RelP and RelQ.
    Steinchen W, Vogt Ms, Altegoer F +4
    Scientific ReportsPeer-reviewedCC BYFull text54 citedStructural biologyGeneral biologyHAL
  4. UPF1 at Work: Structural and Mechanistic Insights Into a Master Regulator of Nonsense-Mediated mRNA Decay
    Vincent Mocquet, Francesca Fiorini
    Journal of Molecular BiologyPeer-reviewedCC BY-NC-ND 4.0Full text1 citedMolecular biology & gene regulationHAL
  5. PslG-Mediated Disruption of Pseudomonas aeruginosa Biofilms: A Multi-Omics Investigation of Matrix Glycan Release, Metabolic Reprogramming, and Structural Disintegration
    Yaqian Zheng, Zebin Gui, Yun Xue +5
    International journal of molecular sciencesPeer-reviewedCC BYFull textMolecular biology & gene regulationEurope PMCCrossref

Cite

BibTeXRIS
BibTeX
@article{patil2026peptidomicsguided,
  title = {{Peptidomics-guided 3D structural-mechanistic investigation of bovine colostrum peptides reveals multi-targeted}},
  author = {Shashank M. Patil and Ramith Ramu and Kalirajan Rajagopal and Vivek Hamse Kameshwar},
  journal = {Food Chemistry: X},
  year = {2026},
  month = oct,
  doi = {10.1016/j.fochx.2026.104454},
  url = {https://doi.org/10.1016/j.fochx.2026.104454},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Peptidomics-guided 3D structural-mechanistic investigation of bovine colostrum peptides reveals multi-targeted
AU  - Shashank M. Patil
AU  - Ramith Ramu
AU  - Kalirajan Rajagopal
AU  - Vivek Hamse Kameshwar
PY  - 2026
DA  - 2026/10/28
JO  - Food Chemistry: X
DO  - 10.1016/j.fochx.2026.104454
UR  - https://doi.org/10.1016/j.fochx.2026.104454
AB  - Multi-target inhibition of α-amylase, α-glucosidase, and human aldose reductase can significantly address postprandial hyperglycemia and subsequent diabetic complications, yet bovine colostrum peptides remain largely unscreened against these enzymes. Using a peptidomics-guided, integrated in silico and in vitro approach, we identified three lead peptides and highlighted Peptide P2 (GPAGPQGPR) as a common lead inhibitor, showing favorable predicted binding and interaction profiles relative to the reference inhibitors. A dedicated 3D-structural analysis, including residue mapping, RMSF profiles, hydrophobicity surfaces, and intramolecular contact networks, suggested that the glycine-proline-rich scaffold of P2 may support predicted conformational adaptability and interactions with multiple enzyme targets. These findings were supported by in vitro enzyme inhibition and kinetic analyses, which indicated that P2 was consistent with a competitive inhibition model, while radical scavenging analysis indicated its antioxidant potential. These findings establish bovine colostrum as a potential multi-target antidiabetic and antioxidant peptide source, and present a structure-informed, reproducible framework for food-derived peptide discovery.
SN  - 2590-1575
ER  -