posted on 2019-04-26, 10:57authored byS Gabbott, V McCoy, K Penkman, M Collins, S Presslee, J Holt, H Grossman, B Wang, M Solórzano Kraemer, X Delclòs, E Peñalver
Ancient protein analysis is a rapidly developing field of research. Proteins ranging in age from
the Quaternary to Jurassic are being used to answer questions about phylogeny, evolution, and
extinction. However, these analyses are sometimes contentious, and focus primarily on large
vertebrates in sedimentary fossilisation environments; there are few studies of protein
preservation in fossils in amber. Here we show exceptionally slow racemisation rates during
thermal degradation experiments of resin enclosed feathers, relative to previous thermal
degradation experiments of ostrich eggshell, coral skeleton, and limpet shell. We also recover
amino acids from two specimens of fossil feathers in amber. The amino acid compositions are
broadly similar to those of degraded feathers, but concentrations are very low, suggesting that
much of the original protein has been degraded and lost. High levels of racemisation in more
apolar, slowly racemising amino acids suggest that some of the amino acids were ancient and
therefore original. Our findings support that the unique fossilisation environment inside amber
shows potential for the recovery of ancient amino acids and proteins.
Funding
This work is part of the aims of the projects CGL2014-52163 and CGL2017-84419 (Ministry of
Economy, Industry and Competitiveness, Spain), and was supported by a Royal Society Newton
International Fellowship (NF150479) to VEM and VolkswagenStiftung [grant number 90 946] to
MSK. VEM is currently supported by a DFG grant (RU 665/13-1, project number 396637283).
Amino acid analyses were undertaken thanks to support from the Leverhulme Trust and Sheila
Taylor. SP was supported by the National Science Foundation under Grant [NSF DEB 1547414].
MJC and BW were supported by the National Natural Science Foundation of China (41572010,
41622201, 41688103) and the Chinese Academy of Sciences (XDPB05).