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Assessing the Extent of Bone Degradation Using Glutamine Deamidation in Collagen

Wilson, Julie, van Doorn, Nienke L., Collins, Matthew J.·2012·Analytical Chemistry
DOI 10.1021/ac301333t
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Abstract

Collagen peptides are analyzed using a low-cost, high-throughput method for assessing deamidation using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). For each chosen peptide, the theoretical distribution is calculated and the measured distribution for each sample compared with this to determine the extent of glutamine deamidation. The deamidation of glutamine (Q) to glutamic acid (E) results in a mass shift of +0.984 Da. Thus, from the resolution of our data, the second peak in the isotope distribution for a peptide containing one glutamine residue coincides with the first peak of the isotope distribution for the peptide in which the residue is deamidated. A genetic algorithm is used to determine the extent of deamidation that gives the best fit to the measured distribution. The method can be extended to peptides containing more than one glutamine residue. The extent of protein degradation assessed in this way could be used, for example, to assess the damage of collagen, and screen samples for radiocarbon dating and DNA analysis.

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  • Deamidation patterns have been explored in multiple archeological substrates, such as collagen degradation in bone, keratin degradation in textiles, and food proteins from ancient dental calculus.

    “Deamidation patterns have therefore been explored in multiple archeological substrates, such as collagen degradation in bone (80, 81), keratin degradation in textiles (82), and food proteins from ancient dental calculus (83).”

    From Ancient protein analysis in archaeology (2021) · cites this paper as [80]

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Metadata

Authors
Wilson, J., van Doorn, N. L., & Collins, M. J.
Affiliations
  • Department of Mathematics, University of York, York YO10 5YW, U.K.
  • BioArCh, Biology (S-Block), University of York, York YO10 5YW, U.K.
Venue
Analytical Chemistry
Publisher
American Chemical Society (ACS)
Published
2012-10-15
Volume
84
Issue
21
Pages
9041-9048
ISSN
  • 0003-2700
  • 1520-6882
DOI
10.1021/ac301333t
Cited by
126
References
1
Language
en

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