@article { ISI:000319221500007,
	title = {Molecular dynamics simulation studies of the structural response of an isolated A beta(1-42) monomer localized in the vicinity of the hydrophilic TiO2 surface},
	journal = {European Biophysics Journal},
	volume = {42},
	number = {6},
	year = {2013},
	month = {JUN},
	pages = {487-494},
	publisher = {SPRINGER},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>We have probed the effect of a model hydrophilic surface, rutile TiO2, on the full-length amyloid beta (A beta(1-42)) monomer using molecular dynamics simulations. The rutile surface brings about sharp changes in the peptide{\textquoteright}s intrinsic behavior in a distance-dependent manner. The intrinsic collapse of the peptide is disrupted, while the beta-sheet propensity is sharply enhanced with increased proximity to the surface. The results may have implications for A beta self-assembly and fibrillogenesis on hydrophilic surfaces and should be taken into consideration in the design of novel nanomaterials for perturbing amyloidogenic behavior.</p>},
	keywords = {Amyloid beta, beta-Sheet propensity, molecular dynamics simulation, TiO2 rutile surface},
	issn = {0175-7571},
	doi = {10.1007/s00249-013-0900-6},
	author = {Jose, Jaya C. and Sengupta, Neelanjana}
}
