21
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      A primer for ZooMS applications in archaeology

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Collagen peptide mass fingerprinting by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry, also known as zooarchaeology by mass spectrometry (ZooMS), is a rapidly growing analytical technique in the fields of archaeology, ecology, and cultural heritage. Minimally destructive and cost effective, ZooMS enables rapid taxonomic identification of large bone assemblages, cultural heritage objects, and other organic materials of animal origin. As its importance grows as both a research and a conservation tool, it is critical to ensure that its expanding body of users understands its fundamental principles, strengths, and limitations. Here, we outline the basic functionality of ZooMS and provide guidance on interpreting collagen spectra from archaeological bones. We further examine the growing potential of applying ZooMS to nonmammalian assemblages, discuss available options for minimally and nondestructive analyses, and explore the potential for peptide mass fingerprinting to be expanded to noncollagenous proteins. We describe the current limitations of the method regarding accessibility, and we propose solutions for the future. Finally, we review the explosive growth of ZooMS over the past decade and highlight the remarkably diverse applications for which the technique is suited.

          Related collections

          Most cited references139

          • Record: found
          • Abstract: found
          • Article: not found

          Collagen structure and stability.

          Collagen is the most abundant protein in animals. This fibrous, structural protein comprises a right-handed bundle of three parallel, left-handed polyproline II-type helices. Much progress has been made in elucidating the structure of collagen triple helices and the physicochemical basis for their stability. New evidence demonstrates that stereoelectronic effects and preorganization play a key role in that stability. The fibrillar structure of type I collagen-the prototypical collagen fibril-has been revealed in detail. Artificial collagen fibrils that display some properties of natural collagen fibrils are now accessible using chemical synthesis and self-assembly. A rapidly emerging understanding of the mechanical and structural properties of native collagen fibrils will guide further development of artificial collagenous materials for biomedicine and nanotechnology.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            The collagen family.

            Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that contain at least one triple-helical domain. Collagens are deposited in the extracellular matrix where most of them form supramolecular assemblies. Four collagens are type II membrane proteins that also exist in a soluble form released from the cell surface by shedding. Collagens play structural roles and contribute to mechanical properties, organization, and shape of tissues. They interact with cells via several receptor families and regulate their proliferation, migration, and differentiation. Some collagens have a restricted tissue distribution and hence specific biological functions.
              Bookmark
              • Record: found
              • Abstract: not found
              • Article: not found

              Bone Collagen Quality Indicators for Palaeodietary and Radiocarbon Measurements

                Bookmark

                Author and article information

                Journal
                Proc Natl Acad Sci U S A
                Proc Natl Acad Sci U S A
                pnas
                pnas
                Proceedings of the National Academy of Sciences of the United States of America
                National Academy of Sciences
                0027-8424
                1091-6490
                10 May 2022
                17 May 2022
                10 May 2022
                : 119
                : 20
                : e2109323119
                Affiliations
                [1] aDepartment of Anthropology, Harvard University , Cambridge, MA 02318;
                [2] bDepartment of Anthropology, Boston University , Boston, MA 02215;
                [3] cDepartment of Archaeogenetics, Max Planck Institute for Evolutionary Anthropology , Leipzig 04103, Germany
                Author notes
                1To whom correspondence may be addressed. Email: kkrichter@ 123456palaeome.org or warinner@ 123456fas.harvard.edu .

                Edited by Suzanne Pilaar Birch, The University of Georgia, Athens, GA; received June 18, 2021; accepted January 14, 2022 by Editorial Board Member Dolores R. Piperno

                Author contributions: K.K.R. and C.W. designed research; K.K.R., M.C.C., M.S., and C.W. performed research; K.K.R. and C.W. analyzed data; and K.K.R., M.C.C., M.S., and C.W. wrote the paper.

                Author information
                https://orcid.org/0000-0001-5617-9415
                https://orcid.org/0000-0002-9651-9514
                https://orcid.org/0000-0002-4528-5877
                Article
                202109323
                10.1073/pnas.2109323119
                9171758
                35537051
                5c2014fe-df17-4ab8-800c-3f5aed1a0674
                Copyright © 2022 the Author(s). Published by PNAS.

                This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY).

                History
                Page count
                Pages: 10
                Funding
                Funded by: EC | H2020 | H2020 Priority Excellent Science | H2020 European Research Council (ERC) 100010663
                Award ID: 804884-DAIRYCULTURES
                Award Recipient : Christina Warinner
                Funded by: Werner Siemens Stiftung
                Award ID: Paleobiotechnology
                Award Recipient : Christina Warinner
                Categories
                402
                414
                447
                549
                Perspective
                Social Sciences
                Anthropology
                Biological Sciences
                Ecology

                mass spectrometry,maldi-tof,peptide mass fingerprinting,zooarchaeology

                Comments

                Comment on this article