TY - JOUR
T1 - Ancient amino acids from fossil feathers in amber
AU - McCoy, Victoria E.
AU - Gabbott, Sarah E.
AU - Penkman, Kirsty
AU - Collins, Matthew J.
AU - Presslee, Samantha
AU - Holt, John
AU - Grossman, Harrison
AU - Wang, Bo
AU - Solórzano Kraemer, Monica M.
AU - Delclòs, Xavier
AU - Peñalver, Enrique
N1 - © 2019, The Author(s).
PY - 2019/4/23
Y1 - 2019/4/23
N2 - 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 indicate that the unique fossilisation environment inside amber shows potential for the recovery of ancient amino acids and proteins.
AB - 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 indicate that the unique fossilisation environment inside amber shows potential for the recovery of ancient amino acids and proteins.
UR - http://www.scopus.com/inward/record.url?scp=85065296106&partnerID=8YFLogxK
U2 - 10.1038/s41598-019-42938-9
DO - 10.1038/s41598-019-42938-9
M3 - Article
C2 - 31015542
AN - SCOPUS:85065296106
SN - 2045-2322
VL - 9
SP - 1
EP - 8
JO - Scientific Reports
JF - Scientific Reports
IS - 1
M1 - 6420
ER -