title: Gastrointestinal endogenous proteins as a source of bioactive peptides--an in silico study.
abstract: Dietary proteins are known to contain bioactive peptides that are released during digestion. Endogenous proteins secreted into the gastrointestinal tract represent a quantitatively greater supply of protein to the gut lumen than those of dietary origin. Many of these endogenous proteins are digested in the gastrointestinal tract but the possibility that these are also a source of bioactive peptides has not been considered. An in silico prediction method was used to test if bioactive peptides could be derived from the gastrointestinal digestion of gut endogenous proteins. Twenty six gut endogenous proteins and seven dietary proteins were evaluated. The peptides present after gastric and intestinal digestion were predicted based on the amino acid sequence of the proteins and the known specificities of the major gastrointestinal proteases. The predicted resultant peptides possessing amino acid sequences identical to those of known bioactive peptides were identified. After gastrointestinal digestion (based on the in silico simulation), the total number of bioactive peptides predicted to be released ranged from 1 (gliadin) to 55 (myosin) for the selected dietary proteins and from 1 (secretin) to 39 (mucin-5AC) for the selected gut endogenous proteins. Within the intact proteins and after simulated gastrointestinal digestion, angiotensin converting enzyme (ACE)-inhibitory peptide sequences were the most frequently observed in both the dietary and endogenous proteins. Among the dietary proteins, after in silico simulated gastrointestinal digestion, myosin was found to have the highest number of ACE-inhibitory peptide sequences (49 peptides), while for the gut endogenous proteins, mucin-5AC had the greatest number of ACE-inhibitory peptide sequences (38 peptides). Gut endogenous proteins may be an important source of bioactive peptides in the gut particularly since gut endogenous proteins represent a quantitatively large and consistent source of protein.
authors.affiliation: Riddet Institute, Massey University, Palmerston North, New Zealand.
authors.forename: Lakshmi A
authors.initials: LA
authors.lastname: Dave
authors.affiliation: Riddet Institute, Massey University, Palmerston North, New Zealand.
authors.forename: Carlos A
authors.initials: CA
authors.lastname: Montoya
authors.affiliation: Riddet Institute, Massey University, Palmerston North, New Zealand.
authors.forename: Shane M
authors.initials: SM
authors.lastname: Rutherfurd
authors.affiliation: Riddet Institute, Massey University, Palmerston North, New Zealand.
authors.forename: Paul J
authors.initials: PJ
authors.lastname: Moughan
mesh_terms: D000595:Amino Acid Sequence; D019295:Computational Biology / Q000379:methods; D004044:Dietary Proteins / Q000378:metabolism; D005768:Gastrointestinal Hormones / Q000737:chemistry / Q000378:metabolism*; D041981:Gastrointestinal Tract / Q000378:metabolism*; D006801:Humans; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D020543:Proteome; D040901:Proteomics / Q000379:methods
chemical_list: D004044:Dietary Proteins; D005768:Gastrointestinal Hormones; D010455:Peptides; D020543:Proteome