F H Silver1, J W Freeman, D DeVore. 1. Division of Biomaterials, Department of Pathology and Laboratory Medicine, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ, USA. silverfr@umdnj.edu
Abstract
BACKGROUND/AIMS: The purpose of this work is to attempt to determine the elastic spring constant for collagen and elastic fibers (elastin) in skin and to determine if the values of these elastic constants are similar to those reported for other tissues. METHODS: We studied the viscoelastic mechanical properties of human skin and dermis by measuring the incremental stress-strain behavior. Elastic stress-strain curves were used to obtain the elastic spring constant of elastin and collagen while the collagen fibril length was obtained from the slope of viscous stress-strain curves. RESULTS: Our results suggest that the elastic spring constant for elastin is about 4.0 MPa while that for collagen is about 4.4 GPa. The former value is similar to that calculated for ligamentum nuchae while the latter value is about 70% of the value found for tendon and self-assembled type I collagen fibers. The differences between the elastic constants for collagen molecules in tendon and skin is hypothesized to reflect the higher molecular tilt angle and lower D period found in skin compared to tendon as well as a shorter fibril length. CONCLUSION: The differences in the collagen types present in skin and tendon may influence collagen self-assembly and the resulting viscoelastic properties.
BACKGROUND/AIMS: The purpose of this work is to attempt to determine the elastic spring constant for collagen and elastic fibers (elastin) in skin and to determine if the values of these elastic constants are similar to those reported for other tissues. METHODS: We studied the viscoelastic mechanical properties of human skin and dermis by measuring the incremental stress-strain behavior. Elastic stress-strain curves were used to obtain the elastic spring constant of elastin and collagen while the collagen fibril length was obtained from the slope of viscous stress-strain curves. RESULTS: Our results suggest that the elastic spring constant for elastin is about 4.0 MPa while that for collagen is about 4.4 GPa. The former value is similar to that calculated for ligamentum nuchae while the latter value is about 70% of the value found for tendon and self-assembled type I collagen fibers. The differences between the elastic constants for collagen molecules in tendon and skin is hypothesized to reflect the higher molecular tilt angle and lower D period found in skin compared to tendon as well as a shorter fibril length. CONCLUSION: The differences in the collagen types present in skin and tendon may influence collagen self-assembly and the resulting viscoelastic properties.
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