A Molecular Simulation Study of the Structure and Self-aggregation of Elastin-like Peptides

Elastin confers elasticity to various vertebrate tissues. Elastin and elastin-like peptides are disordered and undergo temperature-induced phase separation. This thesis focuses on two studies of monomeric elastin-like peptides. In the first study, we combine molecular dynamics simulations, nuclear magnetic resonance, and small-angle x-ray scattering to analyze the structure of an elastin-like peptide containing alternating hydrophobic and cross-linking domains reminiscent of elastin. Simulation and experimental results are consistent in terms of local but not global structural properties. The ability of simulations to generate a high resolution structural ensemble allows more precise determination of structural propensities from experimental observables. In the second study, we use molecular dynamics simulations to investigate the temperature dependence of the structural properties of elastin-like peptides. The structural ensemble is governed by the hydrophobic effect and chain entropy. The results are not consistent with models of elastin’s self-aggregation that involves a structural ordering in monomers with increasing temperature.M.Sc