Marek Janko1,2, Albert Zink2,3, Alexander M. Gigler1,2, Wolfgang M. Heckl1,2,4 and Robert W. Stark1,2,*
-Author Affiliations
1Department of Earth and Environmental Sciences, Ludwig-Maximilians-Universität München, Theresienstraße 41, 80333 Munich, Germany
2Center for NanoSciences, Ludwig-Maximilians-Universität München,Schellingstraße 4, 80799 Munich, Germany
3European Academy of Bolzano, Institute for Mummies and the Iceman,Viale Druso 1, 39100 Bolzano, Italy
4Deutsches Museum, Museumsinsel 1, 80538 Munich, Germany
*Author for correspondence (stark@lmu.de).
Abstract
Skin protects the body from pathogens and degradation. Mummified skin in particular is extremely resistant to decomposition. External influences or the action of micro-organisms, however, can degrade the connective tissue and lay the subjacent tissue open. To determine the degree of tissue preservation in mummified human skin and, in particular, the reason for its durability, we investigated the structural integrity of its main protein, type I collagen. We extracted samples from the Neolithic glacier mummy known as ‘the Iceman’. Atomic force microscopy (AFM) revealed collagen fibrils that had characteristic banding patterns of 69 ± 5 nm periodicity. Both the microstructure and the ultrastructure of dermal collagen bundles and fibrils were largely unaltered and extremely well preserved by the natural conservation process. Raman spectra of the ancient collagen indicated that there were no significant modifications in the molecular structure. However, AFM nanoindentation measurements showed slight changes in the mechanical behaviour of the fibrils. Young's modulus of single mummified fibrils was 4.1 ± 1.1 GPa, whereas the elasticity of recent collagen averages 3.2 ± 1.0 GPa. The excellent preservation of the collagen indicates that dehydration owing to freeze-drying of the collagen is the main process in mummification and that the influence of the degradation processes can be addressed, even after 5300 years.
2Center for NanoSciences, Ludwig-Maximilians-Universität München,Schellingstraße 4, 80799 Munich, Germany
3European Academy of Bolzano, Institute for Mummies and the Iceman,Viale Druso 1, 39100 Bolzano, Italy
4Deutsches Museum, Museumsinsel 1, 80538 Munich, Germany
*Author for correspondence (stark@lmu.de).
Abstract
Skin protects the body from pathogens and degradation. Mummified skin in particular is extremely resistant to decomposition. External influences or the action of micro-organisms, however, can degrade the connective tissue and lay the subjacent tissue open. To determine the degree of tissue preservation in mummified human skin and, in particular, the reason for its durability, we investigated the structural integrity of its main protein, type I collagen. We extracted samples from the Neolithic glacier mummy known as ‘the Iceman’. Atomic force microscopy (AFM) revealed collagen fibrils that had characteristic banding patterns of 69 ± 5 nm periodicity. Both the microstructure and the ultrastructure of dermal collagen bundles and fibrils were largely unaltered and extremely well preserved by the natural conservation process. Raman spectra of the ancient collagen indicated that there were no significant modifications in the molecular structure. However, AFM nanoindentation measurements showed slight changes in the mechanical behaviour of the fibrils. Young's modulus of single mummified fibrils was 4.1 ± 1.1 GPa, whereas the elasticity of recent collagen averages 3.2 ± 1.0 GPa. The excellent preservation of the collagen indicates that dehydration owing to freeze-drying of the collagen is the main process in mummification and that the influence of the degradation processes can be addressed, even after 5300 years.
ancient collagen degradation atomic force microscopy nanoindentation Raman spectroscopy Iceman
Footnotes
Received February 23, 2010.
Accepted March 4, 2010.
This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
© 2010 The Royal Society
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