Biomechanical properties of collagens studied by brillouin light scattering spectroscopy and atomic force microscopy

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