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- Title
Label-Free Method Development for Hydroxyproline PTM Mapping in Human Plasma Proteome.
- Authors
Dutta, Debabrata; Rahman, Shakilur; Bhattacharje, Gourab; Bag, Swarnendu; Sing, Bidhan Chandra; Chatterjee, Jyotirmoy; Basak, Amit; Das, Amit Kumar
- Abstract
Post-translational modifications (PTMs) impart structural heterogeneities that can alter plasma proteins' functions in various pathophysiological processes. However, the identification and mapping of PTMs in untargeted plasma proteomics is still a challenge due to the presence of diverse components in blood. Here, we report a label-free method for identifying and mapping hydroxylated proteins using tandem mass spectrometry (MS/MS) in the human plasma sample. Our untargeted proteomics approach led us to identify 676 de novo sequenced peptides in human plasma that correspond to 201 proteins, out of which 11 plasma proteins were found to be hydroxylated. Among these hydroxylated proteins, Immunoglobulin A1 (IgA1) heavy chain was found to be modified at residue 285 (Pro285 to Hyp285), which was further validated by MS/MS study. Molecular dynamics (MD) simulation analysis demonstrated that this proline hydroxylation in IgA1 caused both local and global structural changes. Overall, this study provides a comprehensive understanding of the protein profile containing Hyp PTMs in human plasma and shows the future perspective of identifying and discriminating Hyp PTM in the normal and the diseased proteomes.
- Subjects
TANDEM mass spectrometry; HYDROXYPROLINE; BLOOD proteins; MOLECULAR dynamics; POST-translational modification
- Publication
Protein Journal, 2021, Vol 40, Issue 5, p741
- ISSN
1572-3887
- Publication type
Article
- DOI
10.1007/s10930-021-09984-7