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.

本研究旨在对犊牛皮来源的市售胶原蛋白（collagen）、猪皮来源的明胶A（gelatine A）以及牛皮来源的明胶B（gelatine B）开展化学表征。本研究采用自下而上蛋白质组学（bottom-up proteomics）方法，包括非均相体系中的胰蛋白酶消化（trypsin digestion）、液相色谱-串联质谱（LC-MS/MS）分析以及生物信息学（bioinformatics）分析，以探究胶原蛋白中关键的化学修饰类型，包括甲硫氨酸（methionine）残基氧化、天冬酰胺（asparagine）与谷氨酰胺（glutamine）脱酰胺，以及多肽链（polypeptide chain）的断裂。我们以市售I型胶原蛋白（collagen type I）及动物皮料来源的明胶作为对照，用于表征一组明胶基动物胶；该组动物胶此前已由Ntasi G.等人（10.17632/hbmc8yhf7y.5）完成分析，由此可开展不同胶黏剂制备方法所产生影响的对比研究。通过阐明不同明胶化（gelatinization）过程中产生的特异性化学修饰模式，本研究旨在揭示这些修饰对胶原蛋白的化学完整性、结构以及黏附性能的影响。