Abstract
The potential of collagens to release biopeptides was evaluated using the BIOPEP-UWM-implemented quantitative criteria including the frequency of the release of fragments with a given activity by selected enzyme(s) (AE), relative frequency of release of fragments with a given activity by selected enzyme(s) (W), and the theoretical degree of hydrolysis (DHt). Cow, pig, sheep, chicken, duck, horse, salmon, rainbow trout, goat, rabbit, and turkey collagens were theoretically hydrolyzed using: stem bromelain, ficin, papain, pepsin, trypsin, chymotrypsin, pepsin+trypsin, and pepsin+trypsin+chymotrypsin. Peptides released from the collagens having comparable AE and W were estimated for their likelihood to be bioactive using PeptideRanker Score. The collagens tested were the best sources of angiotensin I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitors. AE and W values revealed that pepsin and/or trypsin were effective producers of such peptides from the majority of the collagens examined. Then, the SwissTargetPrediction program was used to estimate the possible interactions of such peptides with enzymes and proteins, whereas ADMETlab was applied to evaluate their safety and drug-likeness properties. Target prediction revealed that the collagen-derived peptides might interact with several human proteins, especially proteinases, but with relatively low probability. In turn, their bioactivity may be limited by their short half-life in the body.
Highlights
Collagen is an extracellular protein being the structural component of connective tissues like skin, bone, cartilage, and tendons [1]
Taking into account the growing scientific interest in the analysis of biological functions of collagen hydrolysates as well as possibilities of studying biomolecules using bioinformatic tools, the aim of this study was the bioinformatic comparison of food protein-derived collagen sequences, including their “in silico” hydrolysates, as sources of biopeptides based on quantitative parameters
Our protocol involving the quantitative parameters used to evaluate the potential of proteins to act as sources of biopeptides (A) and to release biopeptides due to the enzyme action (AE, W, and DHt )
Summary
Collagen is an extracellular protein being the structural component of connective tissues like skin, bone, cartilage, and tendons [1]. The structural nature of collagen was described by Gómez-Guillén et al [5]. It consists of three α-chains forming a triple helix stabilized by hydrogen bonds [5]. All collagen types contain the G-P-Hyp repetitive sequential motif, where G stands for glycine, P for proline (mostly), and Hyp for hydroxyl-proline/hydroxyl-lysine. This motif is responsible for the triple helical structure and rigidity of the molecule [4].
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