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Site‐specific deamidation of glutamine: a new marker of bone collagen deterioration
Author(s) -
Doorn Nienke L.,
Wilson Julie,
Hollund Hege,
Soressi Marie,
Collins Matthew J.
Publication year - 2012
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.6351
Subject(s) - deamidation , chemistry , mass spectrometry , glutamine , biochemistry , chromatography , enzyme , amino acid
RATIONALE Non‐enzymatic deamidation accumulates in aging tissues in vivo and has been proposed to be potentially useful as a molecular clock. The process continues post mortem, and here we explore the increase in levels of deamidation in archaeological collagen, as measured during Zooarchaeology by Mass Spectrometry (ZooMS) analysis. METHODS With the high sensitivity of current generation mass spectrometers, ZooMS provides a non‐destructive and highly cost‐effective method to characterise collagen peptides. Deamidation can be detected by mass spectrometry as a +0.984 Da mass shift; therefore, aside from its original purpose, peptide mass‐fingerprinting for bone identification, ZooMS concurrently yields a 'thermal indicator' of the samples. RESULTS By analysis of conventional ZooMS spectra, we determined the deamidation rate for glutamine residues in 911 bone collagen samples from 50 sites, with ages varying from medieval to Palaeolithic. The degree of deamidation was compared to diagenetic parameters and nearby sequence properties. CONCLUSIONS The extent of deamidation was found to be influenced more by burial conditions and thermal age than, for example, chronological age, the extent of bioerosion or crystallinity. The method lends itself mostly to screening heterogenic deposits of bone to identify outliers. Copyright © 2012 John Wiley & Sons, Ltd.