Molecular Dynamics Study of the Solvation and Mechanical Properties of Elastin-like Peptides

Elastin is a disordered structural protein that imparts extensibility and elastic recoil to major arteries, lungs, and other elastic human tissues. Elastin-based peptides are biocompatible and able to self-assemble, making them suitable for biomimetic materials. Recent studies have begun to uncover the role of entropic effects, including the hydrophobic effect and conformational entropy, in the structural ensemble of elastin-like peptides. In this study, we use atomistic molecular dynamics simulations of peptides based on the hydrophobic domains of elastin to investigate their solvation and mechanical properties. The modulus of elastin-like domains obtained from equilibrium fluctuations is commensurate with elastic measurements from simulations as they are pulled to full extension and subsequently allowed to collapse. Our findings indicate that the hydrophobic effect is a significant driving force for elastic recoil, and suggest that the isolated hydrophobic domains are not responsible for the low resilience of elastin-based materials.M.Sc