Aβ42 fraction in the heterogeneous oligomers increases dramatically over time but not Aβ40.

<p>(A) The size of Aβ40 in the heterogeneous species (as indicated by the green arrow) shifts to smaller species after 48 hours (Mann-Whitney U test, p = 8.6E-7). (B) The size of Aβ42 in the heterogeneous species (as indicated by the red arrow) increases considerably up to 48 hours (Mann-Whitney U test, p = 6.3E-7). (C) The ratio was calculated by dividing the number of Aβ42 monomer by the number of Aβ40 monomer in each individual heterogeneous species. The dashed line indicates ratio 1 at which value the amount of Aβ42 is equal to Aβ40. Data was calculated from two different experiments, at least 5 images each. Each image contained at least 50 oligomers. Error bars represent standard deviation of the mean.</p

Diagram of the number of Aβ40 and Aβ42 oligomers on the neurites.

<p>The color assignments are the same as in Figure 4. Green and red circles represent the total number of Aβ40 and Aβ42 species respectively (including both homogeneous and heterogeneous species). The overlap region of the two circles (brown area) represents the heterogeneous species. And the blue circle inside the brown area represents those heterogeneous species that do not show FRET signal. At 10 minutes, there are slightly more Aβ42 species than Aβ40, therefore larger red circle. By 48 hours, the number of Aβ40 species remains similar; therefore the green circle remains the same. The number of Aβ42 species increases over 48 hours (the dashed red circle depicts the population at 10 minutes). Since additional Aβ42 also binds to homogeneous Aβ40, the fraction of heterogeneous species among Aβ40 increase (unpaired two-tailed t-test, **P < 0.05), and the fraction of homogeneous Aβ40 decreases over 48 hours.</p

Aβ40 or Aβ42 oligomers form mainly dimers and show little growth on neurites.

<p>2nM Aβ40-HL555 or Aβ42-HL647 was incubated with primary hippocampal neurons for 10 minutes and 48 hours before imaging. Comparison of the oligomeric size distribution between 10 minutes and 48 hours shows limited growth for both Aβ40-HL555 (Mann-Whitney U test, p > 0.1) and Aβ42-HL647 (Mann-Whitney U test, p = 0.001). The distribution is normalized to total Aβ oligomers. Percentages of each condition were calculated from two different experiments, 5 images each. Each image contained at least 50 oligomers. Error bars represent standard deviation of the mean. The percent is obtained by normalizing to the total number of oligomers. </p

Heterogeneous oligomers are larger than homogeneous oligomers.

<p>(A) Homogeneous Aβ40 remains mainly dimeric on the neurites over 48 hours. (B) Homogeneous Aβ42 also forms mainly dimeric with slight increase in size over 48 hours. (C) Heterogeneous species contains mainly trimer and tetramer and many other oligomers larger than heptamer. The size of heterogeneous species was calculated by summing the number of Aβ40 and Aβ42 in that particular mixture. Percentages of each condition were calculated from two different experiments, at least 5 images each. Each image contained at least 50 oligomers. Error bars represent standard deviation of the mean. </p

Summary of synergistic interactions between Aβ40 and Aβ42 on the neurons.

<p>For Aβ40, the total number of membrane bound oligomers (including both homogeneous and heterogeneous species) does not change, suggesting either no solution Aβ40 binds to the membrane or the association and dissociation of solution Aβ40 to the membrane reach the equilibrium. Size of homogeneous Aβ40 remains mostly dimeric. For Aβ42, the total number of membrane bound oligomers increases. Solution Aβ42 preferentially binds heterogeneous species, increasing the Aβ42/Aβ40 ratio in each mixture. Solution Aβ42 also binds to homogeneous Aβ40, increasing the number of heterogeneous species and shifting the fraction of Aβ40 in the heterogeneous oligomer to a slightly smaller species. However, the solution Aβ42 forms new oligomers and also binds to homogeneous Aβ42, therefore maintaining the size of homogeneous Aβ42 unchanged. </p

Heterogeneous species increases over time due to continuous binding of Aβ42 to the neurites.

<p>2 nM Aβ40 and 2 nM Aβ42 were mixed and incubated with cultured neurons at the same time. By comparing the population changes of each species, we get general idea of how these species interact over time. (A) The relative number of oligomers of each species in each sample (percentage of each species). The blue shading (colocalization without FRET) represents the co-localized Aβ40 and Aβ42 that do not show a FRET signal. This species accounts for at most 10% for both Aβ40 and Aβ42. The green shaded sections represent the percentage of homogeneous Aβ40 in total Aβ40 species, and show the fraction of homogeneous Aβ40 to decrease over time. The red bar represents the percentage of homogeneous Aβ42 in total Aβ42 species. This number remains almost unchanged over time, indicating the fraction of homogeneous Aβ42 remains unchanged. The brown bar represents the percentage of heterogeneous mixed species in total Aβ40 (left two) or Aβ42 (right two) species. The fraction of heterogeneous species among the whole Aβ40 species increases over time (from 35% to 45%), whereas the fraction of heterogeneous species among whole Aβ42 species remains similar. (B) The density (number of Aβ42 per 100 µm) of Aβ42 oligomers on the neurites (including both homogeneous and heterogeneous species) is slightly higher than Aβ40 at 10 minutes and becomes significantly larger by 48 hours, whereas the total number of Aβ40 is only slightly changed (unpaired two-tailed t-test, *P > 0.1 and **P < 0.05). Data was averaged from two different experiments, at least 5 images each and each image contained at least 50 oligomers. Error bars represent standard deviation of the mean. Figure 5 provides a pictorial display of the implications.</p

Bilayer Metasurfaces for Dual- and Broadband Optical Antireflection

Optical antireflection has long been pursued for a wide range of applications, but existing approaches encounter issues in the performance, bandwidth, and structure complexity, particularly in the long-wavelength infrared regime. Here we present the demonstration of bilayer metasurfaces that accomplish dual- and broadband optical antireflection in the terahertz and mid-infrared spectral ranges. By simply tailoring the structural geometry and dimensions, we show that subwavelength metal/dielectric structures enable dramatic reduction of Fresnel reflection and significant enhancement of transmission at a substrate surface, operating either at two discrete narrow bands or over a broad bandwidth up to 28%. We also use a semianalytical interference model to interpret the obtained results, in which we find that the dispersion of the constituent structures plays a critical role in achieving the observed broadband optical antireflection

Supplementary Figure 1 and Table 1 from Membrane capacitance of thousands of single white blood cells

Figure 1: Pattern recognition using neural network for classifying granulocytes and lymphocytes based on Cspec (a) and Cmem (b) where (i-x) represent confusion matrix from ten individual donors and xi represents all the data in combination.;Table 1: A summary of the Cspec (μF/cm2) and Cmem (pF) of granulocytes and lymphocytes from ten healthy donors with the results of neural network based pattern recognition included (cell segmentation number (n)=11). Note that error bars represent standard deviations of the measurement results