01489nas a2200217   4500008004100000022001400041245013800055210006900193260005700262300001200319490000700331520063900338653001800977653002000995653001901015653003401034653002701068100002401095700002501119856012701144       2012                        eng d  a0175-757100aEffect of the A30P mutation on the structural dynamics of micelle-bound alpha synuclein released in water: a molecular dynamics study0 aEffect of the A30P mutation on the structural dynamics of micell  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcMAY  a483-4890 v413 a<p>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.</p>10aA30P mutation10aAlpha synuclein10aKink formation10amolecular dynamics simulation10aStructural persistence1 aChatterjee, Prathit1 aSengupta, Neelanjana  uhttps://library.ncl.res.in/content/effect-a30p-mutation-structural-dynamics-micelle-bound-alpha-synuclein-released-water-001491nas a2200205   4500008004100000022001400041245016300055210006900218260005700287300001200344490000700356520065200363653001701015653002601032653003401058653002401092100001901116700002501135856012501160       2013                        eng d  a0175-757100aMolecular dynamics simulation studies of the structural response of an isolated A beta(1-42) monomer localized in the vicinity of the hydrophilic TiO2 surface0 aMolecular dynamics simulation studies of the structural response  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcJUN  a487-4940 v423 a<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'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>10aAmyloid beta10abeta-Sheet propensity10amolecular dynamics simulation10aTiO2 rutile surface1 aJose, Jaya, C.1 aSengupta, Neelanjana  uhttps://library.ncl.res.in/content/molecular-dynamics-simulation-studies-structural-response-isolated-beta1-42-monomer-002056nas a2200229   4500008004100000022001400041245012700055210006900182260007300251300001200324490000800336520116700344653001501511653002501526653002001551653002101571653003401592653002901626100001901655700002501674856012701699       2013                        eng d  a0301-462200aSurface induced collapse of A beta(1-42) with the F19A replacement following adsorption on a single walled carbon nanotube0 aSurface induced collapse of A beta142 with the F19A replacement   aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcDEC  a108-1150 v1843 a<p>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's initial nucleation and self-assembly. We report here the effects of sharply reducing both aromatic and hydrophobic character within the peptide'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'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.</p>10aAdsorption10aAmyloid beta peptide10acarbon nanotube10aLateral mobility10amolecular dynamics simulation10aSurface induced collapse1 aJana, Asis, K.1 aSengupta, Neelanjana  uhttps://library.ncl.res.in/content/surface-induced-collapse-beta1-42-f19a-replacement-following-adsorption-single-walled-0