Abstract
The toxicity of antimony (Sb) is closely related to its chemical forms. To further realize the toxicity risk of different forms of Sb, the separate and simultaneous binding mechanisms of antimony potassium tartrate/potassium pyroantimonate with bovine serum albumin (BSA) were investigated with muti-spectroscopic methods. Fluorescence quenching result and UV–vis absorption spectra showed that a 1:1 complex was formed between antimony potassium tartrate/potassium pyroantimonate and BSA through a modest binding force. The results revealed that the binding of antimony potassium tartrate/potassium pyroantimonate to BSA caused changes in the secondary structure of BSA. Both Sb forms (antimony potassium tartrate and potassium pyroantimonate) were able to interact with BSA when coexisting but there was a binding influence on their interacting with the BSA. Both Sb forms interfere with the binding of the other to protein.
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References
Abdelhameed AS, Alanazi AM, Bakheit AH, Darwish HW, Ghabbour HA, Darwish IA (2017) Fluorescence spectroscopic and molecular docking studies of the binding interaction between the new anaplastic lymphoma kinase inhibitor crizotinib and bovine serum albumin. Spectrochim Acta A Mol Biomol Spectrosc 171:174–182. https://doi.org/10.1016/j.saa.2016.08.005
Adams RL, Broughton KS (2016) Insulinotropic effects of whey: mechanisms of action, recent clinical trials, and clinical applications. Ann Nutr Metab 69:56–63. https://doi.org/10.1159/000448665
Agrawal R, Siddiqi MK, Thakur Y, Tripathi M, Asatkar AK, Khan RH, Pande R (2019) Explication of bovine serum albumin binding with naphthyl hydroxamic acids using a multispectroscopic and molecular docking approach along with its antioxidant activity. Luminescence 34:628–643. https://doi.org/10.1002/bio.3645
Alhazmi HA (2019) FT-IR spectroscopy for the identification of binding sites and measurements of the binding interactions of important metal ions with bovine serum albumin. Sci Pharm 87:1–13. https://doi.org/10.3390/scipharm87010005
Barakat C, Patra D (2013) Combining time-resolved fluorescence with synchronous fluorescence spectroscopy to study bovine serum albumin-curcumin complex during unfolding and refolding processes. Luminescence 28:149–155. https://doi.org/10.1002/bio.2354
Bolaños K, Kogan MJ, Araya E (2019) Capping gold nanoparticles with albumin to improve their biomedical properties. Int J Nanomed 14:6387–6406. https://doi.org/10.2147/ijn.s210992
Cao H, Yi Y (2017) Study on the interaction of chromate with bovine serum albumin by spectroscopic method. Biometals 30:529–539. https://doi.org/10.1007/s10534-017-0022-1
Chen Z, Zhang J, Liu C (2013) Study on the interaction between a water-soluble dinuclear nickel complex and bovine serum albumin by spectroscopic techniques. Biometals 26:827–838. https://doi.org/10.1007/s10534-013-9663-x
Chen M, Liu Y, Cao H, Song L, Zhang Q (2015) The secondary and aggregation structural changes of BSA induced by trivalent chromium: a biophysical study. J Lumin 158:116–124. https://doi.org/10.1016/j.jlumin.2014.09.021
Chunmei D, Cunwei J, Huixiang L, Yuze S, Wei Y, Dan Z (2014) Study of the interaction between mercury (II) and bovine serum albumin by spectroscopic methods. Environ Toxicol Pharmacol 37:870–877. https://doi.org/10.1016/j.etap.2014.01.021
Das S, Bora N, Rohman MA, Sharma R, Jha AN, Roy AS (2018) Molecular recognition of bio-active flavonoids quercetin and rutin by bovine hemoglobin: an overview of the binding mechanism, thermodynamics and structural aspects through multi-spectroscopic and molecular dynamics simulation studies. Phys Chem Chem Phys 20:21668–21684. https://doi.org/10.1039/c8cp02760a
Das S, Pahari S, Sarmah S, Rohman MA, Paul D, Jana M, Roy AS (2019) Lysozyme–luteolin binding: molecular insights into the complexation process and the inhibitory effects of luteolin towards protein modification. Phys Chem Chem Phys 21:12649–12666. https://doi.org/10.1039/c9cp01128e
Deng L, Sun N, Kitova EN, Klassen JS (2010) Direct quantification of protein− metal ion affinities by electrospray ionization mass spectrometry. Anal Chem 82:2170–2174. https://doi.org/10.1021/ac902633d
Fan J, Sun W, Wang Z, Peng X, Li Y, Cao J (2014) A fluorescent probe for site I binding and sensitive discrimination of HSA from BSA. Chem Commun 50:9573–9576. https://doi.org/10.1039/c4cc03778b
Förster T (1948) Zwischenmolekulare energiewanderung und fluoreszenz. Ann Phys 437:55–75. https://doi.org/10.1002/andp.19484370105
Ghosh S, Paul BK, Chattopadhyay N (2014) Interaction of cyclodextrins with human and bovine serum albumins: A combined spectroscopic and computational investigation. Int J Chem Sci 126:931–944. https://doi.org/10.1007/s12039-014-0652-6
Guo W, Fu Z, Wang H, Liu S, Wu F, Giesy JP (2018) Removal of antimonate (Sb(V)) and antimonite (Sb(III)) from aqueous solutions by coagulation-flocculation-sedimentation (CFS): Dependence on influencing factors and insights into removal mechanisms. Sci Total Environ 644:1277–1285. https://doi.org/10.1016/j.scitotenv.2018.07.034
Hoogenboezem EN, Duvall CL (2018) Harnessing albumin as a carrier for cancer therapies. Adv Drug Deliv Rev 130:73–89. https://doi.org/10.1016/j.addr.2018.07.011
Lakowicz JR (2006) Principles of Fluorescence Spectroscopy. Springer, New York
Li W, Fu F, Ding Z, Tang B (2018) Zero valent iron as an electron transfer agent in a reaction system based on zero valent iron/magnetite nanocomposites for adsorption and oxidation of Sb (III). J Taiwan Inst Chem Eng 85:155–164. https://doi.org/10.1016/j.jtice.2018.01.032
Li XF, Ma LG, Yang YQ, Liu YJ, Meng XR, Yang HX (2020) Synthesis, crystal structure and bovine serum albumin–binding studies of a new Cd (II) complex incorporating 2, 2′-(propane-1, 3-diyl) bis (1H-imidazole-4, 5-dicarboxylate). Acc Chem Res 44:198–205. https://doi.org/10.1177/1747519819895240
Litvinov RI, Faizullin DA, Zuev YF, Weisel JW (2012) The α-helix to β-sheet transition in stretched and compressed hydrated fibrin clots. Biophys J 103:1020–1027. https://doi.org/10.1016/j.bpj.2012.07.046
Lloyd JBF (1971) Synchronized excitation of fluorescence emission spectra. Nat Phys Sci 231:64–65. https://doi.org/10.1038/physci231064a0
Long X, Wang X, Guo X, He M (2020) A review of removal technology for antimony in aqueous solution. J Environ Sci 90:189–204. https://doi.org/10.1016/j.jes.2019.12.008
Ma GJ, Ferhan AR, Jackman JA, Cho NJ (2020) Conformational flexibility of fatty acid-free bovine serum albumin proteins enables superior antifouling coatings. Comms Mat 1:1–11. https://doi.org/10.1038/s43246-020-0047-9
Meti MD, Nandibewoor ST, Joshi SD, More UA, Chimatadar SA (2015) Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin. J Pharm Anal 5:249–255. https://doi.org/10.1016/j.jpha.2015.01.004
Moreno-Andrade I, Regidor-Alfageme E, Durazo A, Field JA, Umlauf K, Sierra-Alvarez R (2020) LC-ICP-OES method for antimony speciation analysis in liquid samples. J Environ Sci Health A 55:457–463. https://doi.org/10.1080/10934529.2019.1707565
Nurdiansyah R, Rifa’i M (2016) A comparative analysis of serum albumin from different species to determine a natural source of albumin that might be useful for human therapy. J Taibah Univ Medical Sci 11:243–249. https://doi.org/10.1016/j.jtumed.2016.04.003
Patel R, Kumari M, Dohare N, Khan AB, Singh P, Malik M, Kumar A (2016) Interaction between pyrrolidinium based ionic liquid and bovine serum albumin: a spectroscopic and molecular docking insight. Anal Biochem 5:1–8. https://doi.org/10.4172/2161-1009.1000265
Paul BK, Bhattacharjee K, Bose S, Guchhait N (2012) A spectroscopic investigation on the interaction of a magnetic ferrofluid with a model plasma protein: effect on the conformation and activity of the protein. Phys Chem Chem Phys 14:15482–15493. https://doi.org/10.1039/c2cp42415k
Paul S, Ghanti R, Sardar PS, Majhi A (2019) Synthesis of a novel coumarin derivative and its binding interaction with serum albumins. Chem Heterocycl Compd (N Y) 55:607–611. https://doi.org/10.1007/s10593-019-02505-6
Pawar SK, Jaldappagari S (2019) Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches. J Pharm Anal 9:274–283. https://doi.org/10.1016/j.jpha.2019.03.007
Petitpas I, Bhattacharya AA, Twine S, East M, Curry S (2001) Crystal structure analysis of warfarin binding to human serum albumin anatomy of drug site I. J Biol Chem 276:22804–22809. https://doi.org/10.1074/jbc.m100575200
Renard F, Putnis CV, Montes-Hernandez G, King HE, Breedveld GD, Okkenhaug G (2018) Sequestration of antimony on calcite observed by time-resolved nanoscale imaging. Environ Sci Technol 52(1):107–113. https://doi.org/10.1021/acs.est.7b04727
Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20:3096–3102. https://doi.org/10.1021/bi00514a017
Roy AS, Samanta SK, Ghosh P, Tripathy DR, Ghosh SK, Dasgupta S (2016) Cell cytotoxicity and serum albumin binding capacity of the morin-Cu (II) complex and its effect on deoxyribonucleic acid. Mol Biosyst 12:2818–2833. https://doi.org/10.1039/c6mb00344c
Sahilli YC, Akgun MH, Yildiz D (2016) Antimony induced glutathione efflux from human erythroctes. Fresenius Environ Bull 25:4965–4971
Samarkina DA, Gabdrakhmanov DR, Lukashenko SS, Nizameev IR, Kadirov MK, Zakharova LY (2019) Homologous series of amphiphiles bearing imidazolium head group: complexation with bovine serum albumin. J Mol Liq 275:232–240. https://doi.org/10.1016/j.molliq.2018.11.082
Shahid M, Khalid S, Dumat C, Pierart A, Niazi NK (2019) Biogeochemistry of antimony in soil-plant system: Ecotoxicology and human health. Appl Geochem 106:45–59. https://doi.org/10.1016/j.apgeochem.2019.04.006
Sharma D, Ojha H, Pathak M, Singh B, Sharma N, Singh A, Kakkar R, Sharma RK (2016) Spectroscopic and molecular modelling studies of binding mechanism of metformin with bovine serum albumin. J Mo Struct 1118:267–274. https://doi.org/10.1016/j.molstruc.2016.04.030
Shi J-H, Lou Y-Y, Zhou K-L, Pan DQ (2018) Spectroscopic and molecular docking approaches for the investigation of molecular interactions between herbicide sulfosulfuron and bovine serum albumin. J Biomol Struct Dyn 36:2822–2830. https://doi.org/10.1080/07391102.2017.1375991
Song W, Zhang D, Pan X, Lee DJ (2013) Complexation of HSA with different forms of antimony (Sb): an application of fluorescence spectroscopy. J Lumin 136:80–85. https://doi.org/10.1016/j.jlumin.2012.11.008
Sundar S, Chakravarty J (2010) Antimony toxicity. Int J Environ Res Public Health 7:4267–4277. https://doi.org/10.3390/ijerph7124267
Tamás MJ, Sharma SK, Ibstedt S, Jacobson T, Christen P (2014) Heavy metals and metalloids as a cause for protein misfolding and aggregation. Biomolecules 4:252–267. https://doi.org/10.3390/biom4010252
Tantimongcolwat T, Prachayasittikul S, Prachayasittikul V (2019) Unravelling the interaction mechanism between clioquinol and bovine serum albumin by multi-spectroscopic and molecular docking approaches. Spectrochim Acta A Mol Biomol Spectrosc 216:25–34. https://doi.org/10.1016/j.saa.2019.03.004
Verdugo M, Ruiz Encinar J, Costa-Fernández JM, Menendez-Miranda M, Bouzas-Ramos D, Bravo M, Quiroz W (2017) Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb (III) and Sb (V). PLoS ONE 12:1–20. https://doi.org/10.1371/journal.pone.0170869
Voit E, Udovenko A, Kovaleva E, Makarenko N, Beleneva I, Zemnukhova L (2019) Structure and properties of the molecular complex of antimony (III) fluoride with γ-glycine. J Struct Chem 60:630–639. https://doi.org/10.1134/S0022476619040140
Wang X, He M, Xi J, Lu X (2011) Antimony distribution and mobility in rivers around the world’s largest antimony mine of Xikuangshan, Hunan Province, China. Microchem J 97:4–11. https://doi.org/10.1016/j.microc.2010.05.011
Wang L, Li H, Yu D, Wang Y, Wang W, Wu M (2019) Hyperbranched polyamide-functionalized sodium alginate microsphere as a novel adsorbent for the removal of antimony (III) in wastewater. Environ Sci Pollut Res 26:27372–27384. https://doi.org/10.1007/s11356-019-05914-4
Wani TA, AlRabiah H, Bakheit AH, Kalam MA, Zargar S (2017) Study of binding interaction of rivaroxaban with bovine serum albumin using multi-spectroscopic and molecular docking approach. Chem Cent J 11:1–9. https://doi.org/10.1186/s13065-017-0366-1
Wilson SC, Lockwood PV, Ashley PM, Tighe M (2010) The chemistry and behaviour of antimony in the soil environment with comparisons to arsenic: A critical review. Environ Pollut 158:1169–1181. https://doi.org/10.1016/j.envpol.2009.10.045
Wu B, Qu C, Wang Y, Zhao J, Du H (2019) Comparison of the quenching effects of two main components of ziziphi spinosae semen on serum albumin fluorescence. J Fluoresc 29:1113–1123. https://doi.org/10.1007/s10895-019-02422-z
Xu X, Zhang L, Shen D, Wu H, Liu Q (2008) Oxygen-dependent oxidation of Fe (II) to Fe (III) and interaction of Fe (III) with bovine serum albumin, leading to a hysteretic effect on the fluorescence of bovine serum albumin. J Fluoresc 18:193–201. https://doi.org/10.1007/s10895-007-0263-4
Yang Y, Feng Y, Wang Y, Wang L, Shi W (2013) Interactions between U (VI) and bovine serum albumin. J Radioanal Nucl Chem 298:903–908. https://doi.org/10.1007/s10967-013-2487-x
Yang Y, Zhang N, Sun Y, Li J, Zhao R, Zheng Z, Ding Y, Zhang X, Geng D, Sun Y (2019) Multispectroscopic and molecular modeling studies on the interaction of bile acids with bovine serum albumin (BSA). J Mol Struct 1180:89–99. https://doi.org/10.1016/j.molstruc.2018.09.004
Yu X, Liu R, Ji D, Yang F, Li X, Xie J, Zhou J, Yi P (2011) Study on the synergism effect of lomefloxacin and ofloxacin for bovine serum albumin in solution by spectroscopic techniques. J Solution Chem 40:521–531. https://doi.org/10.1007/s10953-011-9653-y
Yue HL, Hu YJ, Huang HG, Jiang S, Tu B (2014) Development of morin-conjugated Au nanoparticles: Exploring the interaction efficiency with BSA using spectroscopic methods. Spectrochim Acta A Mol Biomol Spectrosc 130:402–410. https://doi.org/10.1016/j.saa.2014.04.022
Zhang Q, Ni Y (2017) Comparative studies on the interaction of nitrofuran antibiotics with bovine serum albumin. Rsc Adv 7:39833–39841. https://doi.org/10.1039/c7ra05570f
Zhang J, Chen W, Tang B, Zhang W, Chen L, Duan Y, Zhu YX, Zhu Y, Zhang Y (2016) Interactions of 1-hydroxypyrene with bovine serum albumin: insights from multi-spectroscopy, docking and molecular dynamics simulation methods. Rsc Adv 6:23622–23633. https://doi.org/10.1039/c6ra00981f
Zhang H, Zhang M, Wang Y, Wang Y, Sun S, Fei Z, Cao J (2018) Effects of selected two noble metal ions in medicine on the structure and activity of bovine serum albumin: a multi-spectral studies. J Lumin 194:519–529. https://doi.org/10.1016/j.jlumin.2017.10.081
Zhao X, Liu R, Teng Y, Liu X (2011) The interaction between Ag+ and bovine serum albumin: a spectroscopic investigation. Sci Total Environ 409:892–897. https://doi.org/10.1016/j.scitotenv.2010.11.004
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Gu, J., Yang, G., Li, X. et al. Difference in the binding mechanism of distinct antimony forms in bovine serum albumin. Biometals 34, 493–510 (2021). https://doi.org/10.1007/s10534-021-00291-3
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DOI: https://doi.org/10.1007/s10534-021-00291-3