esponding to the C155-Gal4 crossing in absence or presence of curcumin at different ages, the fraction of the peaks at 508 nm and 543 nm verses the peaks at 508 
nm and 612 nm were analyzed by the GraphPad Prism 5.0 d software. The spectral shifts were estimated as the medium fraction with the standard deviation and compared using two-tailed student’s t-test of unpaired samples. At least five different brains of the different genotypes at different time points were analyzed. The number of spectra taken was dependent on amount of amyloids detected. At least 15 spectra were collected of every genotype at the different time points. In vitro Fibrillation Assay Recombinant Ab142 HFIP was dissolved in 2 mM NaOH into a concentration of 1 mg/ml. The peptide was stored at 220uC. 10 mM Ab142 HFIP was allowed to fibrillate in a 96-well assay plate in 10 mM phosphate buffer pH 7.5 in the absence or presence of curcumin in concentrations of 0.27, 2.7, and 27 mM dissolved in EtOH 0.0001%, 0.001%, and 0.01% added curcumin). The fibrillation was performed at 37uC, at 500 rpm. Aliquots were withdrawn at time points of 0, 60, and 180 GSK126 manufacturer minutes and were assayed by Western blotting and transmission electron microcopy. The p-FTAA fluorescence assay was performed as described in. Native PAGE Western blotting 15 ml aliquots from the fibrillation assay at time points; 0, 60, and 180 minutes, were mixed with 15 ml Native sample buffer and run on a 12% acrylamide gel during native condition. Pre-stained protein standards and synthetic Ab142 peptide were used to indicate the apparent molecular weights of peptides and aggregates. After electrophoresis, proteins were blotted onto ImmobilonP transfer 21753854” membrane set at 100 V for 1 hours at room temperature. After transfer, membranes were rinsed in distilled water followed by blocking using 4% BSA/TBST for 2 hours at room temperature. Blocked membranes were incubated with Monoclonal mouse anti-Amyloid b116 antibody diluted 1:10 000 in 4% BSA/TBST for 1 hours at room temperature. After incubation with primary antibody, membranes were washed three times for 10 minutes in TBST, incubated with alkaline phosphatase-conjugate anti-mouse IgG, diluted 1:1 000 in 4% BSA/TBST for 30 minutes at room temperature, and washed again three times for 10 minutes in TBST. The membrane was developed using Immun-StarTM Chemiluminescent and visualized using a LAS-400mini attached with a CCDcamera. The in vitro fibril formation assay was repeated at three different occasions with fresh solutions. Quantification of the Ab142-peptide in aged Drosophila Five fly heads of newly eclosed, ten and twenty day old double inserted Ab142 expressing flies and newly eclosed, five and ten day old Ab142 E22G expressing flies, both corresponding to the C155Gal4 crossing, were homogenized in 50 ml of extraction buffer ). The homogenate was incubated at room temperature for 10 min, sonicated for 4 minutes in a water bath and then centrifuged at 12 000 g for 5 minutes into a “soluble”and “insoluble”fraction. 20 ml of the supernatant was mixed with 180 ml hepes dilution buffer ). The pellet was homogenized in 50 ml of extraction buffer containing guanidinium 18089725” HCl ). 20 ml of the supernatant of the “insoluble fraction”was mixed with 180 ml hepes dilution buffer prior to analysis. All homogenate samples were assayed in triplicates at three independent assay occasions. The quantification of Ab-peptides in the “soluble”and “insoluble”fractions were performed using the M
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