Role of Surface Charge of Inhibitors on Amyloid Beta Fibrillation

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1 Supporting Information Role of Surface Charge of Inhibitors on Amyloid Beta Fibrillation SWATHI SUDHAKAR, PANDURANGAN KALIPILLAI, POORNIMA BUDIME SANTHOSH, ETHAYARAJA MANI* POLYMER ENGINEERING AND COLLOID SCIENCE LABORATORY, DEPARTMENT OF CHEMICAL ENGINEERING, INDIAN INSTITUTE OF TECHNOLOGY, MADRAS-00 0, INDIA S1

2 Contents 1. Synthesis of citrate- and CTAB-coated AuNP... S. Characterization of AuNP..... S. ATR-FTIR studies for secondary structure prediction of protein S. Cell viability studies S. Effect of serum proteins on the charge of nanoparticles. S. References S S

3 1. Synthesis of citrate and CTAB coated AuNP AuNP were synthesized according to the Turkevich method. 1 Briefly, 0 ml of 0. mm of HAuCl solution was taken and ml of. mm trisodium citrate solution was added and the mixture was heated to 0 º C for min. In case of CTAB mediated synthesis, ml of CTAB in toluene solution (1 mm) was mixed with ml of 0. % by volume of aqueous solution of HAuCl under continuous stirring. After separating the aqueous yellow phase, sodium borohydride solution of 0. mm was added dropwise until the observation of a clear ruby red color Characterization of AuNP UV-visible spectrometer was used to confirm the chemical composition of the NP. The UV-VIS spectra for citrate-capped and CTAB-capped AuNP, given in the Figure. S1-A showed a characteristic peak around nm. Dynamic light scattering was used to measure the hydrodynamic diameter and the zeta potential measurements were performed using Zetasizer component in the DLS. The hydrodynamic diameter (d) and zeta (ζ) potentialfor citrate-capped AUNP are d = 1 ± nm and ζ potential = -0 mv; and for CTAB-capped AuNP, d = 1 ± nm and ζ potential = + mv. The morphology of the NP were examined using transmission electron microscopy (TEM) (Technai G Transmission Electron Microscope (FEI, USA). TEM images of respective AuNPs are shown in Figure S1-b and c. 0 1 S

4 Figure S1. (a) UV Vis absorption spectra of citrate and CTAB stabilized AuNP. TEM images of (b) citrate coated AuNP and (c) TEM images of CTAB coated AuNP. S

5 1. ATR-FTIR studies for secondary structure prediction of protein To predict the secondary structure content and conformational changes occurred in Aβ (1-0) due to the negatively charged AuNP and surfactants, ATR FTIR (Attenuated Total Reflectance - Fourier Transform Infrared, Bruker) spectroscopic studies was carried out. The samples treated with AuNP and DMPC were collected and about 0 µl of the sample was placed in the sample holder with the help of a capillary tube. The spectra were read from 0 cm -1 to 0 cm -1. Figure S shows the time evolution of secondary structure contents of the protein in the absence of and in the presence of AuNP. After treating the sample with the AuNP, the beta structure content decreased from.% to %, however the alpha helical content increased from % to % at 1 st h (Figure S). The same trend was observed on treating the amyloid with DMPC. A significant drop in beta structure and rise in alpha helical content was observed in the protein sample treated with 1 mm DMPC at 1 st hour (Figure. S) S

6 a 1 b Figure S. Secondary structure content (in percentage) at different time hours like 0 h, 1 h and 1 h in the (a) absence and (b) presence of citrate-aunp. S

7 Figure S. Secondary structure content (in percentage) at 1 h in the absence and presence of 1 mm DMPC. Cell viability Assay The toxicity of the citrate AuNPs with multiple cell lines such as T, MCF-, SHSY-Y and HMEC-1 were tested and the cell viability decreased from 0% to %, %, % and 1 % at h for T, MCF-, SHSY-Y and HMEC-1 cells (See Figure S). Figure S and S shows the viability of the cells incubated with a protein solution treated with Silica NP and with surfactant DMPC. Even though silica NP inhibited the amyloid fibril formation, the cell viability 1 S

8 decreased, probably, due to the toxic nature of the silica NP (see Figure S). It is noted that the cell viability increased from % to % at h, 0% to % at h, % to % at h and % to 0 % at h, when the protein samples treated with DMPC (see Figure S). Figure S. Cell viability percentage of different cell lines after treating with nm citrate coated AuNP at different time intervals. 1 1 S

9 Figure S. Cell viability (percentage) in a) the solution of amyloid fibrils b) in the protein solution treated with nm silica NP and c) in the solution containing only nm silica NP. The data is given for three different incubation times. S

10 Figure S. Cell viability (percentage) in a) the solution of amyloid fibrils b) in the protein solution treated with 0.1 mm DMPC, c) in the protein solution treated with 1 mm DMPC and d) in the pure aqueous solution of 1 mm DMPC. The data is given for three different incubation times.. Effect of serum proteins on the charge of nanoparticles To assess the changes due to serum proteins, 1 ml of human serum was incubated with the different concentration of nanoparticles say 1.,.,.0,.0 and.0 nm for about h. Then S

11 the particles were separated by centrifuging at 000 rpm for 1 min. The nanoparticles were separated and characterized using UV and TEM. The zeta potential was also measured using zeta sizer before and after treating with serum proteins. Then nanoparticles treated with serum was taken and mixed with 0 µm of Aβ, in a 1:1 ratio (% v/v). At different time intervals, ThT Fluorescent assay was done and changes in the intensities were monitored for every 1 h up to 0 h. There is no significant increase in the size, as the UV spectrum red shifted only to - nm which was shown in the figure S-a. This shows that protein adsorption on nanoparticle is insignificant. This may be due to the size of gold nanoparticle in the range of 1 nm which is too small to interact with the serum proteins. The result was in correlation with Wang et al, who reported that small nanoparticles will have lower protein adsorption due their higher curvature that reduced the protein binding capacity. TEM images of AuNP after treating with serum proteins also depicted in the figure S-b. The zeta potential value of the treated particles was - ± mv while the untreated particles zeta potential value was -0 ± mv. These measurements suggest that the change in the surface potential in the presence of serum protein solution is insignificant, as the difference in the values are within the range of statistical error in the measurements. Further, kinetics of amyloid fibrillation was studied with different concentration of serum treated citrate-au nanoparticles. As shown in Fig. S-c, the inhibitory effect of the particles is still retained. From these new sets of experiments, we infer that the inhibitory role of nanoparticles and the effect of charges in vivo studies may be similar (qualitatively) to the in vitro study as long as the particle size is small (~ 1 nm). S

12 a 1 b S1

13 c 1 Figure S. (a) UV Vis absorption spectra of serum treated citrate coated AuNP. TEM images of (b) citrate treated citrate coated AuNP and (c) Fibrillation kinetics of Aβ protein incubated with different concentration of serum treated citrate-capped negatively charged AuNP, measured in terms of ThT intensity S1

14 References (1) Dobrowolska, P.; Krajewska A.; Rączka, M.G., Bartosewicz, B.;Nyga, P.;Jankiewicz, B.J. Application of Turkevich method for AUNP synthesis to fabrication of and Core shell nanostructures. Materials. 01,, -. () Cheng, W.; Dong, S.; Wang,E. Langmuir. Synthesis and selfassembly of cetyltrimethylammonium bromide-capped AUNP.Langmuir.00,1, -. () Wang, P.; Wang, X.; Wang, L.; Hou, X.; Liu, W.; Chen, C. Interaction of gold nanoparticle with proteins and cells. Sci. Technol. Adv. Mater. 01, 1, -. () Wang, S. S. S.; Chen, Y. T.; Chou, S. W. Inhibition of Amyloid Fibril Formation of β- Amyloid Peptides via the Amphiphilic Surfactants. Biochim. Biophys. Acta - Mol. Basis Dis.00,, 0 1. () Das, P.; Kang, S. G.; Temple, S.; Belfort, G.; Kim, Y.; Park, J.-H.; Lee, H.; Nam, J.-M. How Do the Size, Charge and Shape of NP Affect Amyloid β Aggregation on Brain Lipid Bilayer? Sci. Rep. 01,, S1

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