TY - JOUR
T1 - Second-harmonic generation imaging of collagen in ancient bone
AU - Thomas, B
AU - McKintosh, D
AU - Fildes, T
AU - Smith, L
AU - Hargrave, F
AU - Islam, Meez
AU - Thompson, Timothy
AU - Layfield, R
AU - Scott, D
AU - Shaw, B
AU - Burrell, C. L
AU - Gonzalez, S
AU - Taylor, S
N1 - Confirmed by author email as Gold open access [20.03.18] For full details see https://www.elsevier.com/about/open-science/open-access
PY - 2017/11/1
Y1 - 2017/11/1
N2 - Second-harmonic generation imaging (SHG) captures triple helical collagen molecules near tissue surfaces. Biomedical research routinely utilizes various imaging software packages to quantify SHG signals for collagen content and distribution estimates in modern tissue samples including bone. For the first time using SHG, samples of modern, medieval, and ice age bones were imaged to test the applicability of SHG to ancient bone from a variety of ages, settings, and taxa. Four independent techniques including Raman spectroscopy, FTIR spectroscopy, radiocarbon dating protocols, and mass spectrometry-based protein sequencing, confirm the presence of protein, consistent with the hypothesis that SHG imaging detects ancient bone collagen. These results suggest that future studies have the potential to use SHG imaging to provide new insights into the composition of ancient bone, to characterize ancient bone disorders, to investigate collagen preservation within and between various taxa, and to monitor collagen decay regimes in different depositional environments.
AB - Second-harmonic generation imaging (SHG) captures triple helical collagen molecules near tissue surfaces. Biomedical research routinely utilizes various imaging software packages to quantify SHG signals for collagen content and distribution estimates in modern tissue samples including bone. For the first time using SHG, samples of modern, medieval, and ice age bones were imaged to test the applicability of SHG to ancient bone from a variety of ages, settings, and taxa. Four independent techniques including Raman spectroscopy, FTIR spectroscopy, radiocarbon dating protocols, and mass spectrometry-based protein sequencing, confirm the presence of protein, consistent with the hypothesis that SHG imaging detects ancient bone collagen. These results suggest that future studies have the potential to use SHG imaging to provide new insights into the composition of ancient bone, to characterize ancient bone disorders, to investigate collagen preservation within and between various taxa, and to monitor collagen decay regimes in different depositional environments.
U2 - 10.1016/j.bonr.2017.10.005
DO - 10.1016/j.bonr.2017.10.005
M3 - Article
SN - 2352-1872
SP - -
JO - Bone Reports
JF - Bone Reports
ER -