Selection of peptide biomarkers in human bone collagen for the evaluation of deamidation (N, Q) and oxidation (M) by targeted proteomics.

We used a dataset of (56) human bones from Herculaneum (22), Pompeii (11), Baia Scalandrone (12), Oplonti (8), and S.Paolo Belsito(3). A shotgun proteomic approach was applied to the samples, and collagen type I chains have always been identified with good scores and confidence. Screening of all the mass spectrometric data was performed in search of the most frequently detected and/or deamidated peptides and the results were analyzed on a statistical basis to select the best peptides to be later used in the quantification of deamidation.