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Peer-reviewedCC BY-NC-ND 4.0ACS Omega

Fractionation and Identification of Bioactive Peptides from Camel Skin Hydrolysate: In Silico and Molecular Docking Analysis

  • Manel Djebbi1
  • Ola Abdelhedi1
  • Takoua Ben Hlel1
  • Marta Gallego2
  • Cristina Moreno-Mariscal2
  • Mourad Jridi1
  • Leticia Mora2
  1. 1University of Jendouba , , ,
  2. 2Instituto de Agroquímica y Tecnología de Alimentos (CSIC) , Avenue Agustín Escardino, 7 , , , ,
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Abstract

Hypertension and glycemia disorders are severe issues in public health, highlighting the urgent need for the discovery of natural bioactive agents with health benefits. In this sense, the present study examines camel skin gelatin hydrolyzate, obtained using Alcalase (GHA). GHA was first ultrafiltrated, and the low molecular weight fraction (<10 kDa) with the highest in vitro ACE and DPP-IV inhibitory activities (82.75% and 72.5%, respectively) was further purified by reversed-phase high-performance liquid chromatography. Among the resulting fractions (FI to FV), FIII and FIV were the most potent inhibitors against the ACE activity. Thus, they were analyzed by LC-MS/MS for peptide identification. In silico and peptidomic analyses revealed several novel peptide sequences. Molecular docking and MM-GBSA studies were subsequently performed to investigate the interactions and estimate the binding energies of the selected peptides with ACE and DPP-IV. Among the investigated peptides, GPSGPSGL and GPSGPR showed the strongest energy-binding scores against the studied enzymes with favorable interactions with their active sites. In conclusion, hydrolyzed camel skin gelatin is a promising source of multifunctional bioactive peptides and a potential natural ingredient for the management of hypertension and glycemic disorders.

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Cite

BibTeXRIS
BibTeX
@article{djebbi2026fractionation,
  title = {{Fractionation and Identification of Bioactive Peptides from Camel Skin Hydrolysate: In Silico and Molecular Docking Analysis}},
  author = {Manel Djebbi and Ola Abdelhedi and Takoua Ben Hlel and Marta Gallego and Cristina Moreno-Mariscal and Mourad Jridi and Leticia Mora},
  journal = {ACS Omega},
  year = {2026},
  month = nov,
  doi = {10.1021/acsomega.6c08152},
  url = {https://pubs.acs.org/acsodf/article/doi/10.1021/acsomega.6c08152/5463350/Fractionation-and-Identification-of-Bioactive},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - Fractionation and Identification of Bioactive Peptides from Camel Skin Hydrolysate: In Silico and Molecular Docking Analysis
AU  - Manel Djebbi
AU  - Ola Abdelhedi
AU  - Takoua Ben Hlel
AU  - Marta Gallego
AU  - Cristina Moreno-Mariscal
AU  - Mourad Jridi
AU  - Leticia Mora
PY  - 2026
DA  - 2026/11/03
JO  - ACS Omega
DO  - 10.1021/acsomega.6c08152
UR  - https://pubs.acs.org/acsodf/article/doi/10.1021/acsomega.6c08152/5463350/Fractionation-and-Identification-of-Bioactive
AB  - Hypertension and glycemia disorders are severe issues in public health, highlighting the urgent need for the discovery of natural bioactive agents with health benefits. In this sense, the present study examines camel skin gelatin hydrolyzate, obtained using Alcalase (GHA). GHA was first ultrafiltrated, and the low molecular weight fraction (<10 kDa) with the highest in vitro ACE and DPP-IV inhibitory activities (82.75% and 72.5%, respectively) was further purified by reversed-phase high-performance liquid chromatography. Among the resulting fractions (FI to FV), FIII and FIV were the most potent inhibitors against the ACE activity. Thus, they were analyzed by LC-MS/MS for peptide identification. In silico and peptidomic analyses revealed several novel peptide sequences. Molecular docking and MM-GBSA studies were subsequently performed to investigate the interactions and estimate the binding energies of the selected peptides with ACE and DPP-IV. Among the investigated peptides, GPSGPSGL and GPSGPR showed the strongest energy-binding scores against the studied enzymes with favorable interactions with their active sites. In conclusion, hydrolyzed camel skin gelatin is a promising source of multifunctional bioactive peptides and a potential natural ingredient for the management of hypertension and glycemic disorders.
SN  - 2470-1343
ER  -