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
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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