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Modeling Deamidation in Sheep α-Keratin Peptides and Application to Archeological Wool Textiles

Solazzo, Caroline, Wilson, Julie, Dyer, Jolon M., Clerens, Stefan, Plowman, Jeffrey E., von Holstein, Isabella, Walton Rogers, Penelope, Peacock, Elizabeth E., Collins, Matthew J.·2014·Analytical Chemistry
DOI 10.1021/ac4026362
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Abstract

Deamidation of glutamine (Q) and asparagine (N) has been recognized as a marker of degradation and aging in ancient proteins. Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) to study deamidation in wool textiles, we identified eight peptides from α-keratin proteins in sheep wool that could potentially be used to assess the level of degradation. For each chosen peptide, the extent of deamidation was determined by comparing the calculated theoretical distribution with the measured distribution using a genetic algorithm that gives the best fit to the measured distribution. Variations in the levels of deamidation were observed between peptides and in modern wool samples buried for up to 8 years in which deamidation levels were relatively low under short-term burial. In contrast, deamidation was higher in archeological textile fragments from medieval sites ranging from the 9th to 13th century in York (United Kingdom) and Newcastle (United Kingdom) and from the 13th to 16th century in Reykholt (Iceland). Major differences were observed between the British and the Icelandic samples, showing a negative correlation between age of samples and levels of deamidation, but highlighting the effect of local environment. In addition, nanoscale liquid chromatography-electrospray ionization tandem mass spectrometry (nanoLC-ESI-MS/MS) data indicated that deamidation in wool's α-keratin was influenced by primary and higher-order structures. Predom…

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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 [82]

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Metadata

Authors
Solazzo, C., Wilson, J., Dyer, J. M., Clerens, S., Plowman, J. E., von Holstein, I., Walton Rogers, P., Peacock, E. E., & Collins, M. J.
Affiliations
  • BioArCh, Biology (S Block), Wentworth Way, University of York, York YO10 5DD, U.K.
  • Department of Mathematics, University of York, York YO10 5YW, U.K.
  • Proteins and Biomaterials, AgResearch Lincoln Research Centre, Private Bag 4749, Christchurch 8140, New Zealand
  • Anglo-Saxon Laboratory, Bootham House, 61 Bootham, York YO30 7BT, U.K.
  • NTNU University Museum, Norwegian University of Science and Technology, NO-7491 Trondheim, Norway
Venue
Analytical Chemistry
Publisher
American Chemical Society (ACS)
Published
2013-12-10
Volume
86
Issue
1
Pages
567-575
ISSN
  • 0003-2700
  • 1520-6882
DOI
10.1021/ac4026362
Cited by
49
References
0
Language
en

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