Orientation Matters: Polarization Dependent IR Spectroscopy of Collagen from Intact Tendon Down to the Single Fibril Level
Autor: | Mustafa Kansiz, Gorkem Bakir, Eoghan Dillon, Kathleen M. Gough, Stefan Mastel, Richard Wiens, Benoit E. Girouard |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
fibrils
Materials science tendon Infrared collagen type I Pharmaceutical Science Infrared spectroscopy 02 engineering and technology Signal-To-Noise Ratio Fibril polarization imaging and spectroscopy Article Analytical Chemistry law.invention lcsh:QD241-441 Tendons 03 medical and health sciences Nuclear magnetic resonance lcsh:Organic chemistry Optical microscope law scattering-type scanning near-field optical microscopy (s-SNOM) Drug Discovery Spectroscopy Fourier Transform Infrared medicine advances in IR imaging Animals Nanotechnology Physical and Theoretical Chemistry Fourier transform infrared spectroscopy Spectroscopy Absorption (electromagnetic radiation) 030304 developmental biology 0303 health sciences Microscopy Organic Chemistry 021001 nanoscience & nanotechnology Tendon optical photothermal spectroscopy (O-PTIR) nano-FTIR spectroscopy far-field infrared spectroscopy medicine.anatomical_structure Chemistry (miscellaneous) Molecular Medicine 0210 nano-technology |
Zdroj: | Molecules Volume 25 Issue 18 Molecules, Vol 25, Iss 4295, p 4295 (2020) |
ISSN: | 1420-3049 |
Popis: | Infrared (IR) spectroscopy has been used for decades to study collagen in mammalian tissues. While many changes in the spectral profiles appear under polarized IR light, the absorption bands are naturally broad because of tissue heterogeneity. A better understanding of the spectra of ordered collagen will aid in the evaluation of disorder in damaged collagen and in scar tissue. To that end, collagen spectra have been acquired with polarized far-field (FF) Fourier Transform Infrared (FTIR) imaging with a Focal Plane Array detector, with the relatively new method of FF optical photothermal IR (O-PTIR), and with nano-FTIR spectroscopy based on scattering-type scanning near-field optical microscopy (s-SNOM). The FF methods were applied to sections of intact tendon with fibers aligned parallel and perpendicular to the polarized light. The O-PTIR and nano-FTIR methods were applied to individual fibrils of 100&ndash 500 nm diameter, yielding the first confirmatory and complementary results on a biopolymer. We observed that the Amide I and II bands from the fibrils were narrower than those from the intact tendon, and that both relative intensities and band shapes were altered. These spectra represent reliable profiles for normal collagen type I fibrils of this dimension, under polarized IR light, and can serve as a benchmark for the study of collagenous tissues. |
Databáze: | OpenAIRE |
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