Mechanical characterization of collagen I fibrils through 3-point bending using AFM (INVITED)

Abstract eng:
Collagen fibrils are the most abundant proteins in the extracellular matrix of biological soft tissue. They contribute to tensile strength as well as mechanical stability, cohesiveness, cellular migration regulation, and remodelling. Collagen fibrils have a characteristic D-banding periodicity of 67 nm. They are synthesized by the assembly of collagen molecules, which have a length of 300 nm and a diameter of 1.4 nm. In the present study, tropocollagen molecules were fibrilized, and 3-point bending tests were performed on ten different samples to evaluate the elastic stiffness of the fibrils. Linear isotropic elasticity was assumed. The Young’s modulus of the collagen fibrils was found to be around 2-3 MPa.

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