Dietary protein peptide bonds

Dietary protein peptide bonds are the covalent amide linkages that connect amino acids within proteins consumed through the diet. In the gastrointestinal tract, these bonds serve as the essential substrate for proteolytic digestion, a process initiated by gastric pepsin and continued by pancreatic enzymes such as trypsin, chymotrypsin, and elastase [1, 2]. The therapeutic relevance of these bonds lies in their role as the target for exogenous enzyme replacement therapies (ERT), such as pancrelipase, which are used to treat malabsorption in conditions like exocrine pancreatic insufficiency (EPI) [3, 4]. Additionally, specific peptide bonds within proline-rich gluten proteins are the focus of novel enzymatic therapies, such as latiglutenase, designed to neutralize immunogenic peptides in Celiac disease [5]. By facilitating the hydrolysis of these bonds, pharmacological interventions aim to ensure proper nutrient absorption and prevent the inflammatory or toxic effects of undigested protein fragments [6]. This target is unique in that it represents a chemical linkage within a broad class of substrates rather than a single biological macromolecule.

Other names

Amide bondsPolypeptide linkagesDietary protein substratesProteolytic cleavage sites

Exogenous proteolytic enzymes catalyze the hydrolysis of peptide bonds, breaking down dietary proteins into absorbable amino acids and small peptides.