Molecular assessment of the elastic properties of collagen-like homotrimer sequences.
Knowledge of the mechanical behavior of collagen molecules is critical for understanding the mechanical properties of collagen fibrils that constitute the main architectural building block of a number of connective tissues. In this study, the elastic properties of four different type I collagen 30-residue long molecular sequences, were studied by performing stretching simulations using the molecular mechanics approach. The energy-molecular length relationship was achieved by means of the geometry optimization procedure for collagen molecule strains up to 10%. The energy was interpolated by a second order function, and the second order of the derivative with respect to the mean length corresponded to the molecule stiffness. According to the hypothesis of linear elastic behavior, except for one sequence, the elastic modulus was around 2.40 GPa. These values are larger than fibril values, and they confirm the hypothesis that tendon mechanical properties are deeply related to tendon hierarchical structure. A possible explanation of the lowest values obtained for one sequence (1.33-1.53 GPa) is provided and discussed.
Vesentini
Simone
S
Department of Bioengineering, Politecnico di Milano, Via Golgi, 39, 20133, Milano, Italy. simone.vesentini@biomed.polimi.it
Fitié
Carel F C
CF
Montevecchi
Franco M
FM
Redaelli
Alberto
A
D001696:Biomechanical Phenomena / Q000379:methods*; D024042:Collagen Type I / Q000737:chemistry*; D003238:Connective Tissue; D019281:Dimerization; D004548:Elasticity; D006801:Humans; D008958:Models, Molecular; D008962:Models, Theoretical; D008968:Molecular Conformation; D011312:Pressure; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D024042:Collagen Type I