Abstract
Viscoelasticity of collagen is essential for the integrity of connective tissue and its aberrancy may result in collagen dysfunction and the emergence of connective tissue diseases. Precise identification of viscoelastic properties of collagens, and affecting factors are necessary to understand collagen behavior in the extracellular matrix as well as the mechanism of collagen-related diseases. The aim of this study is to investigate the mechanical and viscoelastic properties and time-lapse changes of protein-protein and protein-solvent hydrogen bonds of proline-rich and hydroxyproline-rich collagens by molecular dynamics simulation applying a virtual creep test. To this end, ten different collagen-like protein structures including [(Gly-Pro-Ala)7]3, [(Gly-Pro-Arg)7]3, [(Gly-Pro-Asp)7]3, [(Gly-Pro-Lys)7]3, [(Gly-Pro-Ser)7]3, [(Gly-Pro-Hyp)7]3, [(Gly-Ala-Hyp)7]3, [(Gly-Glu-Hyp)7]3, [(Gly-Leu-Hyp)7]3 and [(Gly-Val-Hyp)7]3 were virtually built and the viscoelastic properties of the structures were determined by virtual creep test according to Kelvin–Voigt model with various constant pulling forces. Different pulling forces ranged from 500 piconewton (pN) to 5000 pN were applied. As a result, Young’s modulus of the collagens was found positively correlated with the pulling force. The viscosity values and relaxation times were negatively correlated. Results also revealed a decreased number of intramolecular hydrogen bonds in hydroxyproline-rich collagens (but not in proline-rich collagens) and an increased number of protein-solvent hydrogen bonds in response to the increasing pulling force. Our results also confirmed that proline and hydroxyproline are the most critical amino acids in determining the collagen viscoelasticity. We suggest that collagen length and mechanical force may be additional important factors for biomechanical properties and behavior of collagen in the extracellular matrix. Communicated by Ramaswamy H. Sarma
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