A Novel Protein Corona Characterization based on the Reflectometric Interference Spectroscopy with Silica Colloidal Crystal Films

doi:10.6023/A20090422

Acta Chimica Sinica ›› 2021, Vol. 79 ›› Issue (3): 338-343.DOI: 10.6023/A20090422 Previous Articles Next Articles

Article

基于二氧化硅胶体晶体薄膜和反射干涉光谱的蛋白冠监测方法

吴峰^a^,^b, 苏倩倩^a^,^b, 周乐乐^a^,^b, 许鹏飞^a^,^b, 董傲^a^,^b, 钱卫平^a^,^b^,^*()

a 东南大学生物电子学国家重点实验室南京 210096
b 东南大学生物科学与医学工程学院南京 210096

投稿日期:2020-09-13 发布日期:2021-02-05
通讯作者: 钱卫平
作者简介:
* E-mail: wqian@seu.edu.cn
基金资助:
项目受国家自然科学基金(21775020); 国家重点研发计划(2017YFE0100200); 国家重点研发计划(2017YFA0205303)

A Novel Protein Corona Characterization based on the Reflectometric Interference Spectroscopy with Silica Colloidal Crystal Films

Feng Wu^a^,^b, Qianqian Su^a^,^b, Lele Zhou^a^,^b, Pengfei Xu^a^,^b, Ao Dong^a^,^b, Weiping Qian^a^,^b^,^*()

a State Key Laboratory of Bioelectronics, Southeast University, Nanjing 210096, China
b School of Biological Science and Medical Engineering, Southeast University, Nanjing 210096, China

Received:2020-09-13 Published:2021-02-05
Contact: Weiping Qian
Supported by:
National Natural Science Foundation of China(21775020); National Key Research and Development Program of China(2017YFE0100200); National Key Research and Development Program of China(2017YFA0205303)

It will form protein corona on the surface of nanoparticles when exposed to the biological environment. The process of protein corona formation is crucial in biomedical engineering, nanomaterials development and research, especially the protein corona formation process of medical engineering materials in blood samples, and there is no mature method for real- time monitoring. Silica colloidal crystal films were prepared by vertical deposition on the glass slides. The glass slides were placed vertically in an ethanol suspension of silica nonospheres with diameters of 110, 190 and 280 nm. After 7 days of ethanol evaporation, a large area of silica colloidal crystal film was formed on the surface of the glass slide. The glass slides of silica colloidal crystal films were assembled into reaction cell, and the reflectometric interference spectroscopy (RIfS) system assembled by microscope light source and spectrometer were used for detection and optical thickness as a parameter. And different concentrations of hydrochloric acid were used to test the performance of the RIfS system. In this study, RIfS was utilized to detect the protein corona formation of human serum albumin, human fibrinogen and immunoglobulin G, as well as blood samples by silica colloidal crystal films which have special optical properties. It was found that the formation of immunoglobulin G had the highest optical thickness variation due to its conformation. According to the formation process of human serum albumin on silica nanosheres with different diameters, the optical thickness of protein corona was also higher on the of silica nanospheres with higher curvature. In addition, through the detection of plasma and whole blood samples, it was found that the silica colloidal crystal films could basically eliminate the interference of blood cells to the detection of protein corona. This work developed a real-time unlabeled protein corona research method, which provides a basis for the clinical application of biomedical materials.

Key words: plasma protein, protein corona, reflectometric interference spectroscopy, silica colloidal crystal film, ordered porous layer interferometry

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Feng Wu, Qianqian Su, Lele Zhou, Pengfei Xu, Ao Dong, Weiping Qian. A Novel Protein Corona Characterization based on the Reflectometric Interference Spectroscopy with Silica Colloidal Crystal Films[J]. Acta Chimica Sinica, 2021, 79(3): 338-343.

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Fig. & Tab. 8

Figure 1. (a) Sectional view SEM image of silica colloidal crystal film with a diameter of 110 nm silica spheres; (b) top view SEM image of silica colloidal crystal film with a diameter of 110 nm ; (c) sectional view SEM image of silica colloidal crystal film with a diameter of 190 nm; (d) top view SEM image of silica colloidal crystal film with a diameter of 190 nm; (e) sectional view SEM image of silica colloidal crystal film with a diameter of 280 nm; (f) top view SEM image of silica colloidal crystal film with a diameter of 280 nm

Figure 2. (a) Typical reflectance interference spectra silica colloidal crystal film of different sphere sizes; (b) photograph of silica colloidal crystal film of different sphere sizes, 110, 190 and 280 nm respectively from left to right

Figure 3. Schematic diagram of protein corona detected device using reflectometric interference spectroscopy based on silica colloidal crystal films

Figure 4. (a) Real-time changes in the optical thickness (ΔOT) of silica colloidal crystal films with perfused ultrapure water, 0.8, 1.2, 1.6 and 2 mol/L of HCl; (b) linear relationship between concentration of HCl and optical thickness variation

Figure 5. (a) Real-time ΔOT caused by different concentrations (2, 1, 0.5, 0.1 and 0.05 mg/mL) of Fg protein corona formation in silica colloidal crystal film; (b) ΔOT caused by different concentration Fg formation of protein corona value at time of 6000 s

Figure 6. A schematic representation of structure and protein corona formation of (a) HSA, (b) Fg and (c) IgG; (d) IgG, HSA and Fg protein corona formation on silica colloidal crystal film and real-time optical thickness changes (ΔOT)

Figure 7. Real-time ΔOT of protein corona formation for HSA at 110, 190 and 280 nm silica colloidal crystal film

Figure 8. Real-time ΔOT of protein corona formation for plasma and whole blood sample at 190 nm silica colloidal crystal film

References 36

[1]	Ma, M.-H; Xu, M.; Liu, S.-J. Acta Chim. Sinica 2020, 78,877. (in Chinese)
	( 马明昊, 徐明, 刘思金, 化学学报, 2020, 78,877.)
[2]	Chakraborty, I.; Pradeep, T. Chem. Rev. 2017, 117,8208. pmid: 28586213
[3]	Cheng, C.; Li, S.; Thomas, A.; Kotov, N. A.; Haag, R. Chem. Rev. 2017, 117,1826. pmid: 28075573
[4]	Shirai, H.; Nguyen, M. T.; Empel, D.; Tsukamoto, H.; Tokunaga, T.; Liao, Y. C.; Yonezawa, T. B. Chem. Soc. Jpn. 2016,20160333.
[5]	Monopoli, M. P.; Berg, C.; Salvati, A.; Dawson, K. A. Nat. Nanotechnol. 2012, 7,779. doi: 10.1038/nnano.2012.207 pmid: 23212421
[6]	Xu, Y.; Zhao, Y.; Zhang, Y.-J.; Cui, Z.-F.; Wang, L.-H.; Fan, C.-H.; Gao, J.-M.; Sun, Y.-H. Acta Chim. Sinica 2018, 76,393. (in Chinese)
	( 徐毅, 赵彦, 张叶俊, 崔之芬, 王丽华, 樊春海, 高基民, 孙艳红, 化学学报, 2018, 76,393.)
[7]	Tenzer, S.; Docter, D.; Kuharev, J.; Musyanovych, A.; Fetz, V.; Hecht, R.; Schlenk, F.; Fischer, D.; Kiouptsi, K.; Reinhardt, C. Nat. Nanotechnol. 2013, 8,772. pmid: 24056901
[8]	Barrán-Berdón, A. L.; Pozzi, D.; Caracciolo, G.; Capriotti, A. L.; Caruso, G.; Cavaliere, C.; Riccioli, A.; Palchetti, S.; Laganà, A. Langmuir 2013, 29,6485. pmid: 23631648
[9]	Ritz, S.; Sch Ttler, S.; Kotman, N.; Baier, G.; Musyanovych, A.; Kuharev, J. R.; Landfester, K.; Schild, H. R.; Jahn, O.; Tenzer, S. Biomacromolecules 2015, 16,1311. pmid: 25794196
[10]	Piella, J.; Bastús, N. G.; Puntes, V. Bioconjug. Chem. 2016,88. doi: 10.1021/bc00013a015 pmid: 1616955
[11]	Zhang, Y.; Wu, J. L. Y.; Lazarovits, J.; Chan, W. C. W. J. Am. Chem. Soc. 2020, 19. ‏ 8827.
[12]	Deng, Z. J.; Liang, M.; Monteiro, M.; Toth, I.; Minchin, R. F. Nat. Nanotechnol. 2011, 6,39. pmid: 21170037
[13]	Fleischer, C. C.; Payne, C. K. Acc. Chem. Res. 2014, 47,2651. pmid: 25014679
[14]	Yan, Y.; Gause, K. T.; Kamphuis, M. M. J.; Ang, C. S.; O Brien-Simpson, N. M.; Lenzo, J. C.; Reynolds, E. C.; Nice, E. C.; Caruso, F. ACS Nano 2013, 7,10960. pmid: 24256422
[15]	Cai, R.; Chen, C. Adv. Mater. 2019, 31,45.
[16]	Brash, J. L. Ann. Ny. Acad. Sci. 2006, 283,356.
[17]	Peppas, N. A. Biomaterials. 1986, 7,239.
[18]	Roach, P.; Farrar, D.; Perry, C. C. J. Am. Chem. Soc. 2005, 127,8168. pmid: 15926845
[19]	Keselowsky, B. G.; Collard, D. M.; A, A. J. G. Biomaterials 2004, 25,5947. doi: 10.1016/j.biomaterials.2004.01.062 pmid: 15183609
[20]	Dupont-Gillain, C. C.; Fauroux, C. M. J.; Gardner, D. C. J. J. Biomed. Mater. Res. A 2003, 67,548. pmid: 14566797
[21]	Baimanov, D.; Wu, J.; Chu, R.; Cai, R.; Chen, C. ACS Nano. 2020, 5,5529.
[22]	Treuel, L.; Eslahian, K. A.; Docter, D.; Lang, T.; Zellner, R.; Nienhaus, K.; Nienhaus, G. U.; Stauber, R. H.; Maskos, M. Phys. Chem. Chem. Phys. 2014, 16,15053. doi: 10.1039/c4cp00058g pmid: 24943742
[23]	Su, Q.; Xu, P.; Zhou, L.; Wu, F.; Dong, A.; Wan, Y.; Qian, W. ACS Appl. Mater. Interfaces 2020, 12,35950. pmid: 32693572
[24]	Choi, H. W.; Sakata, Y.; Kurihara, Y.; Ooya, T.; Takeuchi, T. Anal. Chim. Acta 2012, 728,64. pmid: 22560282
[25]	Murata, A.; Ooya, T.; Takeuchi, T. Microchim. Acta 2015, 182,307.
[26]	Choi, H. W.; Takahashi, H.; Ooya, T.; Takeuchi, T. Anal. Methods-UK. 2011, 3,1366.
[27]	Birkert, O.; Gauglitz, G. Anal. Bioanal. Chem. 2002, 372,141. pmid: 11939184
[28]	Grohmann, S.; Rothe, H.; Eisenhuth, S.; Hoffmann, C.; Liefeith, K. Biointerphases 2011, 6,54. pmid: 21721840
[29]	Merkl, S.; Vornicescu, D.; Dassinger, N.; Kehrel, M.; Harpel, S.; Keusgen, M. Phys. Stat. Sol. 2012, 209,864.
[30]	Fujimura, T.; Takenaka, K.; Goto, Y. Jpn. J. Appl. Phys. 2005, 97,8.
[31]	Tan, Y.; Yang, K.-J.; Cao, Y.-X.; Zhou, R.; Chen, M.; Qian, W.-P. Acta Chim. Sinica 2004, 62,2089. (in Chinese)
	( 谈勇, 杨可靖, 曹跃霞, 周蓉, 陈明, 钱卫平, 化学学报, 2004, 62,2089.)
[32]	Su, Q.; Wu, F.; Xu, P.; Dong, A.; Liu, C.; Wan, Y.; Qian, W. Anal. Chem. 2019, 9,6080.
[33]	Zhou, L.; Su, Q.; Wu, F.; Wan, Y.; Xu, P.; Dong, A.; Li, Q.; Qian, W. Anal. Chem. 2020, 92,12071. doi: 10.1021/acs.analchem.0c02749 pmid: 32786477
[34]	Kraus, G.; Gauglitz, G. Fresenius' J. Anal. Chem. 1994, 5,399.
[35]	Green, R. J.; Davies, J.; Davies, M. C.; Roberts, C. J.; Tendler, S. J. B. Biomaterials 1997, 18,405. pmid: 9061181
[36]	Roach, P.; Farrar, D.; Perry, C. C. J. Am. Chem. Soc. 2006, 128,3939. doi: 10.1021/ja056278e pmid: 16551101

基于二氧化硅胶体晶体薄膜和反射干涉光谱的蛋白冠监测方法

A Novel Protein Corona Characterization based on the Reflectometric Interference Spectroscopy with Silica Colloidal Crystal Films

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