Hydrophobic hydration is an important source of elasticity in elastin-based biopolymers.
Molecular dynamics simulations with explicit waters have been employed to investigate the dominant source of elastin's elasticity. An elastin-like peptide, (VPGVG)(18), was pulled and released in molecular dynamics simulations, at 10 and 42 degrees C, lasting several nanoseconds, which is consistent with the experimentally determined dielectric and NMR relaxation time scales. At elastin's physiological temperature and degree of extension, the simulations indicate that the orientational entropy of waters hydrating hydrophobic groups decreases during pulling of the molecule, but it increases upon release. In contrast, the main-chain fluctuations and other measures of mobility suggest that elastin's backbone is more dynamic in the extended than released state. These results and the agreement between the simulations with various experimental observations suggest that hydrophobic hydration is an important source of the entropy-based elasticity of elastin. Moreover, elastin tends to reorder itself to form a hydrophobic globule when it was held in its extended state, indicating that the hydrophobic effect also contributes in the holding process. On the whole, our simulations support the hydrophobic mechanism of elasticity and provide a framework for description of the molecular basis of this phenomenon.
Li
B
B
Department of Medicinal Chemistry, University of Washington, Seattle, Washington 98195-7610, USA.
Alonso
D O
DO
Bennion
B J
BJ
Daggett
V
V
D001704:Biopolymers / Q000737:chemistry*; D003198:Computer Simulation; D004548:Elasticity; D004549:Elastin / Q000031:analogs & derivatives* / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D014867:Water / Q000737:chemistry
D001704:Biopolymers; D010446:Peptide Fragments; D014867:Water; D004549:Elastin