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Influence of pH on the Spectral-Luminescent Characteristics of the Soft Protein Crown of Silver Nanoparticles
https://doi.org/10.47612/0514-7506-2022-89-2-230-237
Abstract
The spectral and fluorescent characteristics of bovine serum albumin (BSA) molecules in the soft crown of silver nanoparticles (AgNP) were studied at different pH values. The formation of BSA + AgNP complexes was established. The coupling constants of the complex (Kass) and the biomolecular rate constants of the BSA fluorescence quenching (Kq) were determined for different pH values. The dependences of Kass and Kq on pH are nonmonotonic with maxima at pH 6.0. The number of binding sites (Hill coefficient (n)) and the thickness of the BSA soft crown (Dd) are also maximal at pH 6.0. At higher and lower pH values (relative to pH 6.0), these parameters decrease. Variations in the parameters of interaction between BSA and AgNP are due to changes in the conformational modifications of the protein (content of the a-helix) and the microenvironment of Tyr and Trp protein residues in the soft crown (hydrophobicity of the protein).
Keywords
Supporting agencies: Работа выполнена в рамках деятельности научно-образовательной школы Московского государственного университета имени М. В. Ломоносова “Фотонные и квантовые технологии. Цифровая медицина”.
About the Authors
F. D. Davidov
M. V. Lomonosov Moscow State University
Russian Federation
Russian Federation
Moscow
A. A. Kuleshova
M. V. Lomonosov Moscow State University
Russian Federation
Russian Federation
Moscow
A. M. Saletsky
M. V. Lomonosov Moscow State University
Russian Federation
Russian Federation
Moscow
References
1. L. Xu, Y. Wang, J. Huang, C. Chen, Z. Wang, H. Xie. Theranostics, 10, N 20 (2020) 8996—9031
2. R. Salomoni, P. Léo, A. Montemor, B. Rinaldi, M. Rodrigues. Nanotechnol. Sci. Appl., N 10 (2017) 115—121
3. S. Saad. Biomedicine, 41, N 2 (2021) 458—464
4. J. Shi, P. W. Kantoff, R. Wooster, O. C. Farokhzad. Nat. Rev. Cancer, 17 (2017) 20—37
5. R. Machado, A. Pironi, R. Alves, A. Dragalzew, I. Dalberto, M. Chorilli. Curr. Med. Chem., 26 (2019) 2108—2146
6. E. Marsich, F. Bellomo, G. Turco, A. Travan, I. Donati, S. Paoletti. J. Mater. Sci. Mater. Med., 24, (2013) 1799—1807
7. I. Lynch, K. A. Dawson. Nano Today, 3, N 40 (2008) 1—2
8. N. Singh, C. Marets, J. Boudon, N. Millot, L. Saviot, L. Maurizi. Nanoscale Adv., 3 (2021) 1209—1229
9. R. Li, Z. W. Wu, Y. Wang, L. Ding, Y. Wang. Biotechnol. Rep., 9 (2016) 46—52
10. E. S.Gorodnichev, A. A. Kuleshova, O. I. Volkova, A. M. Saletsky. Laser Phys., 31, N 6 (2021) 065601
11. P. Bélteky, A. Rónavári, N. Igaz, B. Szerencsés, I. Y. Tóth, I. Pfeiffer, M. Kiricsi, Z. Kónya. Int. J. Nanomed., 14 (2019) 667—687
12. I. M. Vlasova, A. M. Saletsky. J. Mol. Struct., 936 (2009) 220—227
13. I. M. Vlasova, A. A. Vlasov, A. M. Saletsky. J. Mol. Struct., 984 (2010) 332—338
14. I. M. Vlasova, E. M. Bukharova, A. A. Kuleshova, A. M. Saletsky. Curr. Appl. Phys., 11 (2011)
15. —1132
16. J. Mariam, P. M. Dongre, D. C. Kothari. J. Fluoresc., 21 (2011) 2193—2199
17. M. Liu, Y. Li, L. Li, X. Sun, J. Li, R. Lu. Журн. прикл. спектр., 88, № 1 (2021) 166 [M. Liu, Y. Li, L. Li, X. Sun, J. Li, R. Lu. J. Appl. Specrt., 88 (2021) 153—165]
18. G. Wang, Y. Lu, H. Hou, Y. Liu. RSC Adv., 7 (2017) 9393—9401
19. M. Waghmare, B. Khade, P. Chaudhari, P. Dongre. J. Nanopart. Res., 20, N 7 (2018) 1—21
20. G. J. Quinlan, G. S. Martin, T. W. Evans. Hepatology, 41 (2005) 1211—1219
21. P. Watson, A. T. Jones, D. J. Stephens. Adv. Drug Deliv. Rev., 57 (2005) 43—61
22. G. K. Vertelov, Y. A. Krutyakov, O. V. Efremenkova, A. Yu. Olenin, G. V. Lisichkin. Nanotechnology, 19, N 35 (2008) 355707
23. J. F. Foster. In: Some Aspects of the Structure and Conformational Properties of Serum Albumin, in Albumin Structure, Functions and Uses, Eds. V. M. Rosenoer, M. Oratz, M. A. Rothschild, Oxford, Pergamon Press (1977) 53—84
24. Z. Chi, B. Hong, X. Ren, K. Cheng, Y. Lu, X. Liu. Spectrosc. Lett., 51, N 6 (2018) 279—286
25. W. Misiuk, M. Jozefowicz. J. Mol. Liquids, 202 (2015) 101—106
26. A. Varlan, M. Hillebrand. Molecules, 15, N 6 (2010) 3905—3919
27. F. Ma, C. Sun, W. Zhou, C. Xu, J. Zhou, G. Wang, X. D. Yang. Spectrochim. Acta A: Mol. Biomol. Spectr., 97, N 6 (2012) 885—891
28. G. Sudlow, D. J. Birkett, D. N. Wade. Mol. Pharmacol., 11 (1975) 824—832
29. A. Sulkowska. J. Mol. Struct., 614 (2002) 227—232
30. X. Feng, Z. Lin, L. Yang, C. Wang, C. Bai. Talanta, 47, N 5 (1998) 1223—1229
31. И. М. Власова, А. А. Власов, А. А. Кулешова, Ю. А. Гордеева, А. М. Салецкий. Журн. физ. химии, 94, № 1 (2020) 114—120
32. S. Naveenraj, S. Anandan. J. Photochem. Photobiol. C: Photochem. Rev., 14 (2013) 53—71
Review
For citations:
Davidov F.D., Kuleshova A.A., Saletsky A.M. Influence of pH on the Spectral-Luminescent Characteristics of the Soft Protein Crown of Silver Nanoparticles. Zhurnal Prikladnoii Spektroskopii. 2022;89(2):230-237. (In Russ.) https://doi.org/10.47612/0514-7506-2022-89-2-230-237
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