Fingerprinting Desmosine-Containing Elastin Peptides
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  • 作者:Christoph U. Schr?der ; Andrea Heinz…
  • 关键词:Fragmentation ; Low ; energy CID ; Marker fragments ; Mass spectrometry ; Native cross ; links ; Pyridinium
  • 刊名:Journal of The American Society for Mass Spectrometry
  • 出版年:2015
  • 出版时间:May 2015
  • 年:2015
  • 卷:26
  • 期:5
  • 页码:762-773
  • 全文大小:1,247 KB
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    26.Todo
  • 作者单位:Christoph U. Schr?der (1)
    Andrea Heinz (1)
    Petra Majovsky (2)
    Christian E. H. Schmelzer (1)

    1. Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany
    2. Proteome Analytics Research Group, Leibniz Institute for Plant Biochemistry, Halle (Saale), Germany
  • 刊物主题:Analytical Chemistry; Biotechnology; Organic Chemistry; Proteomics; Bioinformatics;
  • 出版者:Springer US
  • ISSN:1879-1123
文摘
Elastin is a vital protein of the extracellular matrix of jawed vertebrates and provides elasticity to numerous tissues. It is secreted in the form of its soluble precursor tropoelastin, which is subsequently cross-linked in the course of the elastic fiber assembly. The process involves the formation of the two tetrafunctional amino acids desmosine (DES) and isodesmosine (IDES), which are unique to elastin. The resulting high degree of cross-linking confers remarkable properties, including mechanical integrity, insolubility, and long-term stability to the protein. These characteristics hinder the structural elucidation of mature elastin. However, MS2 data of linear and cross-linked peptides released by proteolysis can provide indirect insights into the structure of elastin. In this study, we performed energy-resolved collision-induced dissociation experiments of DES, IDES, their derivatives, and DES-/IDES-containing peptides to determine characteristic product ions. It was found that all investigated compounds yielded the same product ion clusters at elevated collision energies. Elemental composition determination using the exact masses of these ions revealed molecular formulas of the type CxHyN, suggesting that the pyridinium core of DES/IDES remains intact even at relatively high collision energies. The finding of these specific product ions enabled the development of a similarity-based scoring algorithm that was successfully applied on LC-MS/MS data of bovine elastin digests for the identification of DES-/IDES-cross-linked peptides. This approach facilitates the straightforward investigation of native cross-links in elastin.

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