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Investigation of the dynamics of proteolysis by pepsin using statistical approaches
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Investigation of the dynamics of proteolysis by pepsin using statistical approaches

Investigation of the dynamics of proteolysis by pepsin using statistical approaches

During digestion, the proteins we eat release amino acids required for human metabolism, as well as potentially bioactive peptides. These releases and their kinetics depend on the characteristics of the proteins, the food containing them, and the specificity of the proteases that successively intervene during digestion. The gastric phase, which initiates the first stages of food deconstruction, is of prime importance for protein digestion, thanks to the action of pepsin, the first protease to intervene.

Peptidomic datasets derived from in vitro protein hydrolysis by pepsin under simulated gastric conditions have been analyzed using original statistical approaches. These analyses have enabled us to re-examine the specificity of pepsin's action and to propose models for predicting protein hydrolysis by this protease.

The influence of :

  • the nature of the amino acids on either side of the hydrolyzed peptide bonds,
  • the physicochemical environment of peptide bonds (secondary structure, hydrophobicity, charge),
  • the presence of disulfide bridges or glycosylation motifs,
  • the state of protein aggregation,

has been demonstrated.

The enhanced comprehension of pepsin's rules of action offers the propspect of precise regulation of the nature of peptides released during the gastric phase, and by extension, potentially in the rest of the digestive process. In particular, processes capable of modifying the physicochemical characteristics of proteins, including aggregation, could ultimately be levers for modulating the course of digestion.

Studentized propensity scores of amino acid residues (identified according to international coding) at the P1 and P1’ positions after 30 s of in vitro pepsin digestion.

Scores de propension des résidus d’acides aminés
© STLO

Collaborations

  • Région Bretagne pour le financement de la Thèse de Ousmane Suwareh (2020-22)

Read more

  • Suwareh O, Causeur D, Jardin J, Briard-Bion V, Le Feunteun S, Pézennec S, Nau F (2021) Statistical modeling of in vitro pepsin specificity. Food Chemistry, 362, 130098, https://doi.org/10.1016/j.foodchem.2021.130098
  • Suwareh O., Causeur D., Le Feunteun S., Jardin J., Briard-Bion V., Pezennec S., Nau F. (2024) Peptide bonds cleaved by pepsin are affected by the morphology of heat-induced ovalbumin aggregates. Food Chemistry 458, 140260. https://doi.org/10.1016/j.foodchem.2024.140260

Contact

Françoise Nau
 

Modification date: 12 May 2025 | Publication date: 12 May 2025 | By: STLO-MHFamelart