Biomechanical properties of collagens studied by brillouin light scattering spectroscopy and atomic force microscopy
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Date
2016-05
Authors
Akilbekova, D.
Alimzhanov, D.
Utegulov, Zh.
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Abstract
Collagen is the most abundant protein in the human body and the main
component of highly organized tissue structures. Its fibrillar structure is responsible for
biomechanical anisotropies in the tissues and their exceptional elastic properties. In the present
work we use Brillouin light scattering (BLS) spectroscopy and atomic force microscopy (AFM)
for probing elastic properties of collagen fibers harvested from different tissues. While BLS
spectroscopy is non-invasive and label-free modality for probing mechanical properties of fibrous
tissues that can give information on structure-function properties of normal and pathological
tissues on micrometer scale, AFM provides elastic property information in contact manner on
nanometer scale
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Keywords
Collagen, orientation, biomechanical, elastic, Brillouin light scattering spectroscopy, atomic force microscopy
Citation
D. Akilbekova, D. Alimzhanov, and Zh. Utegulov. 2016. Biomechanical properties of collagens studied by brillouin light scattering spectroscopy and atomic force microscopy. Abstract book. 4 th International Scientific Conference “Regenerative medicine & healthy aging”. National Laboratory Astana, Nazarbayev University. http://nur.nu.edu.kz/handle/123456789/1510