Direct Exosome Quantification via Bivalent-Cholesterol-Labeled
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1 SUPPORTING INFORMATION Direct Exosome Quantification via Bivalent-Cholesterol-Labeled DNA Anchor for Signal Amplification Fang He, Hui Liu, Xinggang Guo, Bin-Cheng Yin*,, and Bang-Ce Ye ξ Lab of Biosystem and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, , China The Third Department of Hepatic Surgery, Eastern Hepatobiliary Surgery Hospital, Shanghai, , China ξ Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, College of Pharmaceuti-cal Sciences, Zhejiang University of Technology, Hangzhou , Zhejiang, China *Corresponding author: Bin-Cheng Yin, Tel/Fax no Table of content: Figure S1.Characterization of exosomes Figure S2. Investigation of the conjugation between B-Chol anchor and exosome membrane Figures S3-S6. Optimization of B-Chol anchor assay without HCR for exosome detection Figure S7. Investigation of the specificity in exosome capture using anti-cd9 Figures S8-S9. Optimization of B-Chol anchor assay with HCR amplification for exosome detection Tables S1-S2. Spike-in experiment by B-Chol anchor assay with and without HCR amplification for exosome detection in 5% diluted UC FBS Table S3. Comparison of our method and recently reported methods References S2 S2 S3-S4 S5 S5-S6 S6 S7 S7-S8 S-1
2 1. Characterization of exosome standard Figure S1. Characterization of exosome size. The size distribution of exosomes purified by exoeasy kit characterized by qnano. The mean diameter of exosome was 101 nm. 2. Investigation of the conjugation between B-Chol anchor and exosome membrane Figure S2. Investigation of the conjugation between B-Chol anchor and exosome membrane. Fluorescence microscope images of the reaction system containing immunomagnetic beads in the absence of exosome (top), or anchor (middle), or with both exosome and anchor present (bottom). S-2
3 3. Optimization of B-Chol anchor assay without HCR for exosome detection Figure S3. Optimization of capture temperature in the proposed system for exosome isolation. (A) Absorption spectra of the reaction system at 4 overnight and at 25 for 2 h in the presence and absence of exosomes. (B) Bar graph of absorbance change ratio 1 responses at the two temperatures. A and A 0 are the absorbances at 450 nm in the presence and absence of exosomes, respectively. Error bars show the standard deviation of three experiments. Figure S4. Optimization of capture time in the proposed system for exosome isolation. (A) Absorption spectral responses of the proposed system obtained at different capture times (2, 4, 8, 14, and 20 h) in the presence and absence of exosomes. (B) Bar graph of absorbance change ratio 1 for the different capture times. A and A 0 are the absorbances at 450 nm in the presence and absence of exosomes, respectively. Error bars show the standard deviation of three experiments. S-3
4 Figure S5. Optimization of anchor concentration in the reaction system. (A) Absorption spectra of the proposed system with B-Chol anchor at different concentrations (100 nm, 500 nm, 1 µm, and 1.5 µm) in the presence and absence of exosomes. (B) Bar graph of absorbance change ratio 1 for the different anchor concentrations. A and A 0 are the absorbances at 450 nm in the presence and absence of exosomes, respectively. Error bars show the standard deviation of three experiments. Figure S6. Optimization of anchor time in the reaction system. (A) The absorption spectra of the reaction system at different anchor times (15, 30, 45, 60, and 90 min) in the presence and absence of exosomes. (B) Bar graph of absorbance change ratio 1 for the different anchor times. A and A 0 are the absorbances at 450 nm in the presence and absence of exosomes, respectively. Error bars show the standard deviation of three experiments. S-4
5 4. Investigation of the specificity in exosome capture using anti-cd9 Figure S7. Specificity investigation. (A) UV-vis absorption spectra of the reaction system using CD9 and IgG isotype as control antibody in the presence and absence of exosomes, respectively. (B) Bar graph of absorbance change ratio 1 corresponding to the data (A). A and A 0 are the absorbances at 450 nm in the presence and absence of exosomes, respectively. Error bars show the standard deviation of three experiments. 5. Optimization of B-Chol anchor assay with HCR amplification for exosome detection Figure S8. Optimization of HCR reaction time in the proposed B-Chol anchor assay with HCR amplification. (A) The absorption spectra of the reaction system with different reaction times (10, 30, 60, 90, and 120 min) in the presence and absence of exosomes. (B) Bar graph of absorbance change ratio 1 for the different reaction time. A and A 0 are the absorbances at 450 nm in the presence and absence of exosomes, respectively. Error bars show the standard deviation of three experiments. S-5
6 Figure S9. Optimization of the number of cholesterol moieties in the anchor for assays with and without HCR amplification for exosome detection. (A) The absorption spectra of two assays with B-Chol and M-Chol anchor in the presence and absence of exosomes. (B) Absorbance change ratio 1 corresponding to the data (A). A and A 0 are the absorbances at 450 nm in the presence and absence of exosomes, respectively. Error bars show the standard deviation of three experiments. 6. Spike-in experiment by B-Chol anchor assay with and without HCR amplification for exosome detection in 5% diluted UC FBS Table S1. Recovery results of exosomes in 5% diluted UC FBS by B-Chol anchor assay without HCR amplification Spiked amount (particles/µl) Detected amount (particles/µl) Recovery (%) CV (%) Table S2. Recovery results of exosomes in 5% diluted UC FBS by B-Chol anchor assay with HCR amplification Spiked amount (particles/µl) Detected amount (particles/µl) Recovery (%) CV (%) S-6
7 7. Comparison of our method and recently reported methods Table S3. Comparison of our method and the recently reported methods for exosome detection Method Recognition element LOD (particles/µl) Assay time Linear range (particles/µl) Reference Nanotetrahedron-assisted electrochemical aptasensor Aptamer 20.9 ~12 h Nano-interfaced microfluidic exosome (nano-imex) Antibody 50 ~130 min platform Quantum dot-based electrochemical detection Electrochemical impedance spectroscopy Electrochemical sandwich immunosensor Antibody 100 ~150 min Antibody 190 ~5 h Antibody 200 ~60 min Alternating current electrohydrodynamic (ac-ehd) induced nanoshearing Antibody ~7 h Microfluidic-based mobile exosome detector (µmed) Antibody ~100 min Integrated magneto-electrochemical sensor Antibody ~48 min (i-mex) Aptasensor based on DNA-capped s-swcnts Aptamer ~40 min Lateral flow immunoassay (LFIA) Antibody ~15 min B-Chol anchor assay with enzyme-linked HCR Antibody and cholesterol ~16.5 h Our method 8. References (1) Wang, S.; Zhang, L.; Wan, S.; Cansiz, S.; Cui, C.; Liu, Y.; Cai, R.; Hong, C.; Teng, I. T.; Shi, M.; Wu, Y.; Dong, Y.; Tan, W. ACS Nano 2017, 11, (2) Zhang, P.; He, M.; Zeng, Y. Lab Chip 2016, 16, (3) Boriachek, K.; Islam, M. N.; Gopalan, V.; Lam, A. K.; Nguyen, N.-T.; Shiddiky, M. J. A. Analyst 2017, 142, (4) Li, Q.; Tofaris, G. K.; Davis, J. J. Anal. Chem. 2017, 89, (5) Doldan, X.; Fagundez, P.; Cayota, A.; Laiz, J.; Tosar, J. P. Anal. Chem. 2016, 88, S-7
8 (6) Vaidyanathan, R.; Naghibosadat, M.; Rauf, S.; Korbie, D.; Carrascosa, L. G.; Shiddiky, M. J.; Trau, M. Anal. Chem. 2014, 86, (7) Ko, J.; Hemphill, M. A.; Gabrieli, D.; Wu, L.; Yelleswarapu, V.; Lawrence, G.; Pennycooke, W.; Singh, A.; Meaney, D. F.; Issadore, D. Sci. Rep. 2016, 6, (8) Jeong, S.; Park, J.; Pathania, D.; Castro, C. M.; Weissleder, R.; Lee, H. ACS Nano 2016, 10, (9) Xia, Y.; Liu, M.; Wang, L.; Yan, A.; He, W.; Chen, M.; Lan, J.; Xu, J.; Guan, L.; Chen, J. Biosens. Bioelectron. 2017, 92, 8. (10) Oliveira-Rodriguez, M.; Lopez-Cobo, S.; Reyburn, H. T.; Costa-Garcia, A.; Lopez-Martin, S.; Yanez-Mo, M.; Cernuda-Morollon, E.; Paschen, A.; Vales-Gomez, M.; Blanco-Lopez, M. C. J. Extracell. Vesicles 2016, 5, S-8
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