Collagen-based and mineralized materials, vibrational spectroscopy and chemical imaging
Raman imaging of the crayfish (A) anterior molar. Light micrographs (B and C) of the analyzed area which covers the transition zone between the apatite and the amorphous mineral phase (indicated by the red rectangle in (B)). Raman imaging of the phosphate distribution (D), carbonate to phosphate intensity ratio (E), and the phosphate peak position (F).
Raman imaging of the crayfish (A) anterior molar. Light micrographs (B and C) of the analyzed area which covers the transition zone between the apatite and the amorphous mineral phase (indicated by the red rectangle in (B)). Raman imaging of the phosphate distribution (D), carbonate to phosphate intensity ratio (E), and the phosphate peak position (F).
My research focus is the development of innovative spectroscopic methodologies, mainly based on Raman and Infra-Red (IR) spectral imaging for the use in characterizing biological tissues and biomimetic materials.
Specifically, I aim to understand the response of biological tissues (such as bone, skin, silk, mussel byssal thread, squid sucker rings, whelk egg capsules, lacewing egg-stalks) to external stimuli (hydration, temperature changes, mechanical load) and link molecular structural organization and composition to the macroscopic physical properties of the material.
Furthermore, I explore fundamental mechanisms of biomineralization by studying specific biological models (bone, bone callus, zebrafish larvae, crayfish gastroliths, sea urchin teeth, stomatopod raptorial appendages). In collaboration with researchers at the Federal Institute for Materials Research and Testing in Berlin (Ira Rabin) I also work on damage assessment of the Dead Sea Scrolls.
Polarized Raman mapping of collagen fibril orientation in the crimp region of an un-stretched, fully hydrated rat tail tendon. The hierarchical structure of collagen (A), an optical microscopy image of the crimp region (B) and its corresponding collagen orientation map (C) with magnified regions of interest (D and E).
Polarized Raman mapping of collagen fibril orientation in the crimp region of an un-stretched, fully hydrated rat tail tendon. The hierarchical structure of collagen (A), an optical microscopy image of the crimp region (B) and its corresponding collagen orientation map (C) with magnified regions of interest (D and E).