@article { ISI:000303018700008, title = {Effect of the A30P mutation on the structural dynamics of micelle-bound alpha synuclein released in water: a molecular dynamics study}, journal = {European Biophysics Journal With Biophysics Letters}, volume = {41}, number = {5}, year = {2012}, month = {MAY}, pages = {483-489}, publisher = {SPRINGER}, address = {233 SPRING ST, NEW YORK, NY 10013 USA}, abstract = {

Atomistic molecular dynamics simulation has been used to probe the effect of the A30P mutation on the structural dynamics of micelle-bound, helical alpha Synuclein when released in an aqueous environment. On the timescales simulated, the effect of the mutation on the secondary structure is restricted to local changes close to the mutation site in the N-terminal helical domain. The changes are transient, and all residues except Lys23 recover their initial structure. The local behavior due to the mutation gives rise to a global difference in the A30P mutant in the form of a permanent kink in the N-terminal helical domain.

}, keywords = {A30P mutation, Alpha synuclein, Kink formation, molecular dynamics simulation, Structural persistence}, issn = {0175-7571}, doi = {10.1007/s00249-012-0803-y}, author = {Chatterjee, Prathit and Sengupta, Neelanjana} } @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 = {

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.

}, 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} } @article { ISI:000328443300015, title = {Surface induced collapse of A beta(1-42) with the F19A replacement following adsorption on a single walled carbon nanotube}, journal = {Biophysical Chemistry}, volume = {184}, year = {2013}, month = {DEC}, pages = {108-115}, publisher = {ELSEVIER SCIENCE BV}, type = {Article}, address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}, abstract = {

Spontaneous adsorption of the A beta peptide on the surface of a single-walled carbon nanotube, resulting in the prevention of its intrinsic propensity to form collapsed states, could be a plausible means to hinder the peptide{\textquoteright}s initial nucleation and self-assembly. We report here the effects of sharply reducing both aromatic and hydrophobic character within the peptide{\textquoteright}s central hydrophobic core on its free and surface behavior. In such an altered peptide, complete surface adsorption is found to induce, rather than prevent, the adsorbed peptide{\textquoteright}s collapse. The weakened surface interactions of the central hydrophobic core allow its greater translational mobility on the surface, thereby facilitating interactions that lead to compaction. Both the adsorption and the subsequent collapse are accompanied by a loss of surface hydration in the modified peptide. We further find that such a two-step dewetting leads to hydration levels comparable to that obtained after compaction of the free peptide. These insights may be leveraged for designing molecular surfaces for disrupting intrinsic A beta behavior. (C) 2013 Elsevier B.V. All rights reserved.

}, keywords = {Adsorption, Amyloid beta peptide, carbon nanotube, Lateral mobility, molecular dynamics simulation, Surface induced collapse}, issn = {0301-4622}, doi = {10.1016/j.bpc.2013.09.008}, author = {Jana, Asis K. and Sengupta, Neelanjana} }