Proteomic characterization of standard collagen derived from calf skin, gelatine A from porcine skin and gelatine B from bovine skin

In our work, we aim to chemically characterize commercial collagen derived from calf skin, gelatine A from porcine skin and gelatine B from bovine skin. A bottom-up proteomics approach, including trypsin digestion in a heterogeneous phase followed by LC-MS/MS analysis and bioinformatics, is employed to investigate key chemical modifications in collagen such as oxidation of methionine residues, deamidation of asparagine and glutamine, and cleavage of the polypeptide chain. Data collected for commercially available collagen type I and gelatin from animal hides have been used as controls for the characterization of a set of gelatine-based animal glues, previously analyzed by Ntasi, G. et al. (10.17632/hbmc8yhf7y.5), allowing for a comparative analysis of the effects of different glue manufacturing methods. By elucidating the specific chemical modifications patterns that occur during various gelatinization processes, this research aims to understand their impact on the chemical integrity, structure and adhesive properties of collagen.