Assessing the degradation of ancient milk proteins through site-specific deamidation patterns
Abstract The origins, prevalence and nature of dairying have been long debated by archaeologists. Within the last decade, new advances in high-resolution mass spectrometry have allowed for the direct detection of milk proteins from archaeological remains, including ceramic residues, dental calculus,...
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Nature Portfolio
2021
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oai:doaj.org-article:149a4d7a3497461a8668a700c07b35042021-12-02T14:21:21ZAssessing the degradation of ancient milk proteins through site-specific deamidation patterns10.1038/s41598-021-87125-x2045-2322https://doaj.org/article/149a4d7a3497461a8668a700c07b35042021-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-87125-xhttps://doaj.org/toc/2045-2322Abstract The origins, prevalence and nature of dairying have been long debated by archaeologists. Within the last decade, new advances in high-resolution mass spectrometry have allowed for the direct detection of milk proteins from archaeological remains, including ceramic residues, dental calculus, and preserved dairy products. Proteins recovered from archaeological remains are susceptible to post-excavation and laboratory contamination, a particular concern for ancient dairying studies as milk proteins such as beta-lactoglobulin (BLG) and caseins are potential laboratory contaminants. Here, we examine how site-specific rates of deamidation (i.e., deamidation occurring in specific positions in the protein chain) can be used to elucidate patterns of peptide degradation, and authenticate ancient milk proteins. First, we characterize site-specific deamidation patterns in modern milk products and experimental samples, confirming that deamidation occurs primarily at low half-time sites. We then compare this to previously published palaeoproteomic data from six studies reporting ancient milk peptides. We confirm that site-specific deamidation rates, on average, are more advanced in BLG recovered from ancient dental calculus and pottery residues. Nevertheless, deamidation rates displayed a high degree of variability, making it challenging to authenticate samples with relatively few milk peptides. We demonstrate that site-specific deamidation is a useful tool for identifying modern contamination but highlight the need for multiple lines of evidence to authenticate ancient protein data.Abigail RamsøeMia CrispinMeaghan MackieKrista McGrathRoman FischerBeatrice DemarchiMatthew J. CollinsJessica HendyCamilla SpellerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021) |
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Medicine R Science Q Abigail Ramsøe Mia Crispin Meaghan Mackie Krista McGrath Roman Fischer Beatrice Demarchi Matthew J. Collins Jessica Hendy Camilla Speller Assessing the degradation of ancient milk proteins through site-specific deamidation patterns |
description |
Abstract The origins, prevalence and nature of dairying have been long debated by archaeologists. Within the last decade, new advances in high-resolution mass spectrometry have allowed for the direct detection of milk proteins from archaeological remains, including ceramic residues, dental calculus, and preserved dairy products. Proteins recovered from archaeological remains are susceptible to post-excavation and laboratory contamination, a particular concern for ancient dairying studies as milk proteins such as beta-lactoglobulin (BLG) and caseins are potential laboratory contaminants. Here, we examine how site-specific rates of deamidation (i.e., deamidation occurring in specific positions in the protein chain) can be used to elucidate patterns of peptide degradation, and authenticate ancient milk proteins. First, we characterize site-specific deamidation patterns in modern milk products and experimental samples, confirming that deamidation occurs primarily at low half-time sites. We then compare this to previously published palaeoproteomic data from six studies reporting ancient milk peptides. We confirm that site-specific deamidation rates, on average, are more advanced in BLG recovered from ancient dental calculus and pottery residues. Nevertheless, deamidation rates displayed a high degree of variability, making it challenging to authenticate samples with relatively few milk peptides. We demonstrate that site-specific deamidation is a useful tool for identifying modern contamination but highlight the need for multiple lines of evidence to authenticate ancient protein data. |
format |
article |
author |
Abigail Ramsøe Mia Crispin Meaghan Mackie Krista McGrath Roman Fischer Beatrice Demarchi Matthew J. Collins Jessica Hendy Camilla Speller |
author_facet |
Abigail Ramsøe Mia Crispin Meaghan Mackie Krista McGrath Roman Fischer Beatrice Demarchi Matthew J. Collins Jessica Hendy Camilla Speller |
author_sort |
Abigail Ramsøe |
title |
Assessing the degradation of ancient milk proteins through site-specific deamidation patterns |
title_short |
Assessing the degradation of ancient milk proteins through site-specific deamidation patterns |
title_full |
Assessing the degradation of ancient milk proteins through site-specific deamidation patterns |
title_fullStr |
Assessing the degradation of ancient milk proteins through site-specific deamidation patterns |
title_full_unstemmed |
Assessing the degradation of ancient milk proteins through site-specific deamidation patterns |
title_sort |
assessing the degradation of ancient milk proteins through site-specific deamidation patterns |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/149a4d7a3497461a8668a700c07b3504 |
work_keys_str_mv |
AT abigailramsøe assessingthedegradationofancientmilkproteinsthroughsitespecificdeamidationpatterns AT miacrispin assessingthedegradationofancientmilkproteinsthroughsitespecificdeamidationpatterns AT meaghanmackie assessingthedegradationofancientmilkproteinsthroughsitespecificdeamidationpatterns AT kristamcgrath assessingthedegradationofancientmilkproteinsthroughsitespecificdeamidationpatterns AT romanfischer assessingthedegradationofancientmilkproteinsthroughsitespecificdeamidationpatterns AT beatricedemarchi assessingthedegradationofancientmilkproteinsthroughsitespecificdeamidationpatterns AT matthewjcollins assessingthedegradationofancientmilkproteinsthroughsitespecificdeamidationpatterns AT jessicahendy assessingthedegradationofancientmilkproteinsthroughsitespecificdeamidationpatterns AT camillaspeller assessingthedegradationofancientmilkproteinsthroughsitespecificdeamidationpatterns |
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