Periodic Reporting for period 2 - Palaeochem (Biomolecular innovation and the evolution of animals: insights from taphonomy and the fossil record)
Berichtszeitraum: 2023-01-01 bis 2024-06-30
What are the limits of the fossil record?
Ancient biomolecules are critically important given their potential to inform on phylogenetic relationships and the processes driving evolutionary change.
Research to date, however:
- lacks cohesion and breadth
- is strongly biased towards bone, and
- often fails to consider the impact of analytical bias and fossilization processes.
What’s the project about?
This proposal sets a new, focussed agenda for the study of ancient biomolecules based on the characterization of thin carbon films preserving the soft tissues of fossil animals.
Targeted chemical analysis of diverse fossils including frontier high-resolution mapping will be informed by a rigorous programme of fossilisation experiments simulating decay and burial, thus generating the first holistic models for the preservation of the evolutionarily important biomolecules keratin, melanin, and collagen in fossil soft tissues through deep time.
What will the project do?
- The research will resolve the fossil record of these key biomolecules, the chemical mechanisms responsible for their preservation, and will accommodate taphonomic biases in evolutionary models.
- This enhanced picture of animal molecular evolution will test hypotheses linking biomolecular innovation with fundamental phenotypic, phylogenetic and ecological transitions, especially relating to the evolution of the tetrapod integument and the origins of animals.
- The research will launch twin experimental facilities for simulating burial that will allow extraction, and in-situ analysis, of reaction products in real time. These facilities will be unique in Europe, consolidating the PI’s team as a keystone global hub for research into ancient biomolecules.
The second major finding from our taphonomic experimental programme relates to the applicability of Raman spectroscopy to the identification of chemical signatures for melanin in thermally altered fossils. Thermally altered geomaterials are generally considered uninformative as the Raman spectrum shows only two broad bands – the D- and G-bands. Our experiments on melanotic and non-melanotic tissues and cellular materials from a broad range of bacterial, algal, fungal, higher plant, arthropod and vertebrate species revealed that the Raman spectrum of all of these biomaterials retains a diagnostic signature despite thermal maturation. These signatures are evident following analysis of Raman spectra using peak deconvolution and statistical analysis of extracted peak parameters. This approach clearly discriminates melanised from non-melanised biomaterials and preliminary data suggest that the approach can discriminate between melanins from different source taxa, i.e. that thermally matured melanins retain a phylogenetic fingerprint. This approach is an exciting new method to identify evidence of melanin in older, thermally matured, fossils.
Our melanin research also includes novel data on other fossils. We identified skin patterning in a fossil moonfish from the Eocene of Bolca; the style of patterning – a series of spots – differs from the stripes of moonfish today and indicates a shift in moonfish ecology since the Eocene.
Another major fossil discovery relates to both melanin and feathers. We discovered branched feathers in a pterosaur from the Cretaceous of Brazil, suggesting that feathers evolved in the common avemetatarsalian ancestor of dinosaurs and pterosaurs in the Early Triassic. Moreover, our analyses of the pterosaur feathers revealed the partitioning of melanosomes with different geometries in feathers of different types. This demonstrates that the pterosaur feathers were being used to generate colour patterns, in turn suggesting that coloration may have been an early functional adaptation of feathers.
Finally, our experimental programme has yielded a major advance in our understanding of the fossil record of keratin proteins. Our taphonomic experiments on feathers, and analysis of the altered feathers using FTIR and XANES, showed that during thermal maturation, feather beta corneous proteins transform to alpha helix structures. This explains the alpha helix signal in some fossil feathers as a simple taphonomic artefact. The experimental data also validate our new chemical data from fossil feathers, which demonstrates that even feathers from the Cretaceous can retain secondary and tertiary protein structure, supporting previous claims of protein preservation in Mesozoic fossils.