Univ. Lille, CNRS UAR 3290─MSAP─Miniaturisation pour la Synthèse, l'Analyse et la Protéomique, Lille F-59000, France.
Université Côte d'Azur, CNRS, CEPAM (UMR 7264), Nice F-06300, France.
J Proteome Res. 2024 Aug 2;23(8):3404-3417. doi: 10.1021/acs.jproteome.4c00083. Epub 2024 Jul 23.
Collagen from paleontological bones is an important organic material for isotopic measurement, radiocarbon analysis, and paleoproteomic analysis to provide information on diet, dating, taxonomy, and phylogeny. Current paleoproteomic methods are destructive and require from a few milligrams to several tens of milligrams of bone for analysis. In many cultures, bones are raw materials for artifacts that are conserved in museums, which hampers damage to these precious objects during sampling. Here, we describe a low-invasive sampling method that identifies collagen, taxonomy, and post-translational modifications from Holocene and Upper Pleistocene bones dated to 130,000 and 150 BC using dermatological skin tape discs for sampling. The sampled bone micropowders were digested following our highly optimized enhanced filter-aided sample preparation protocol and then analyzed by MALDI FTICR MS and LC-MS/MS for identifying the genus taxa of the bones. We show that this low-invasive sampling does not deteriorate the bones and achieves results similar to those obtained by more destructive sampling. Moreover, this sampling method can be carried out at archeological sites or in museums.
古生物骨骼中的胶原蛋白是进行同位素测量、放射性碳分析和古蛋白质组分析的重要有机材料,可提供有关饮食、年代测定、分类学和系统发育的信息。目前的古蛋白质组学方法具有破坏性,需要从几毫克到几十毫克的骨骼进行分析。在许多文化中,骨骼是博物馆中保存的文物的原材料,这阻碍了在采样过程中对这些珍贵物品的损坏。在这里,我们描述了一种低侵入性的采样方法,该方法使用皮肤科用的胶带盘从全新世和更新世的骨骼中提取胶原蛋白、分类学和翻译后修饰,这些骨骼的年代为公元前 13 万年至公元前 150 年。对采集的骨微粉进行消化,然后根据我们高度优化的增强过滤辅助样品制备方案进行 MALDI FTICR MS 和 LC-MS/MS 分析,以鉴定骨骼的属种分类。我们表明,这种低侵入性采样不会使骨骼恶化,并获得与更具破坏性采样相似的结果。此外,这种采样方法可以在考古遗址或博物馆进行。