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.

本研究旨在对三类商用动物源胶原材料进行化学表征，分别为小牛皮来源的胶原蛋白、猪皮来源的明胶A以及牛皮来源的明胶B。本研究采用自下而上蛋白质组学（bottom-up proteomics）分析策略，具体涵盖非均相体系胰蛋白酶酶解、液相色谱-串联质谱（LC-MS/MS）检测及生物信息学分析，以探究胶原蛋白的关键化学修饰类型，包括甲硫氨酸残基氧化、天冬酰胺与谷氨酰胺脱酰胺反应，以及多肽链断裂。本研究以市售动物皮源Ⅰ型胶原蛋白与明胶作为对照样本，用于表征一批此前由Ntasi, G.等人（10.17632/hbmc8yhf7y.5）完成分析的明胶基动物胶，进而可开展不同制胶工艺对胶料性能影响的对比分析。通过阐明不同明胶化过程中胶原蛋白所形成的特征化学修饰模式，本研究旨在揭示此类修饰对胶原蛋白化学完整性、分子结构及黏附性能的影响。