The applications and limitations of a minimally destructive approach to archaeological proteomics
Although protein-based studies within archaeology have been applied for many years for bulk analyses, archaeological proteomics is a recent application. Not only can protein mass fingerprinting aid in identification of animal origin, it can reveal new information on the degradation process of proteins. This study will focus on the MALDI-TOF-MS application ZooMS (Zooarchaeology by Mass Spectrometry) on collagen. Primarily collagen extracted from bone, although other collagenous materials were explored, notably leather. Although most bulk analyses protocols require decalcification prior to collagen extraction, and the first iterations of ZooMS analyses did also, this work presents a minimally destructive method to extract collagen from bone, involving extraction with ammonium bicarbonate buffer. The yield is consequentially lower than with a decalcified sample, however, the current generation of ~soft~-ionization mass spectrometers is sufficiently sensitive for peptide fingerprinting these buffer extracts. This allows us to investigate bone samples without loss of the protective mineral fraction. The contribution of this method is especially relevant to archaeological studies as it allows to (re-)investigate
van Doorn, Nienke
The applications and limitations of a minimally destructive approach to archaeological proteomics. Although protein-based studies within archaeology have been applied for many years for bulk analyses, archaeological proteomics is a recent application. Not only can protein mass fingerprinting aid in identification of animal origin, it can reveal new information on the degradation process of proteins. This study will focus on the MALDI-TOF-MS application ZooMS (Zooarchaeology by Mass Spectrometry) on collagen. Primarily collagen extracted from bone, although other collagenous materials were explored, notably leather. Although most bulk analyses protocols require decalcification prior to collagen extraction, and the first iterations of ZooMS analyses did also, this work presents a minimally destructive method to extract collagen from bone, involving extraction with ammonium bicarbonate buffer. The yield is consequentially lower than with a decalcified sample, however, the current generation of ~soft~-ionization mass spectrometers is sufficiently sensitive for peptide fingerprinting these buffer extracts. This allows us to investigate bone samples without loss of the protective mineral fraction. The contribution of this method is especially relevant to archaeological studies as it allows to (re-)investigate
application limitation minimally destructive archaeological proteomics although protein based study within_archaeology apply bulk analysis archaeological proteomics recent application protein mass fingerprint aid identification animal origin reveal new_information degradation process protein study_focus application collagen primarily collagen extract bone although material explore notably although bulk analysis protocols require prior collagen extraction first analysis also work_present minimally destructive method extract collagen bone involve extraction buffer yield low sample however current generation soft mass sufficiently sensitive fingerprint buffer extract allows investigate bone_sample without loss protective mineral fraction method especially relevant_archaeological study allow investigate