References
- Abdullah, S. M. S., Fatma, S., Rabbani, G., & Ashraf, J. M. (2017). A spectroscopic and molecular docking approach on the binding of tinzaparin sodium with human serum albumin. Journal of Molecular Structure, 1127, 283–288. https://doi.org/https://doi.org/10.1016/j.molstruc.2016.07.108
- Acero, J. L., Benitez, J. F., Real, F. J., Leal, A. I., & Sordo, A. (2005). Oxidation of esculetin, a model pollutant present in cork processing wastewaters, by chemical methods, Ozone: Science & Engineering. Ozone: Science & Engineering, 27(4), 317–326. https://doi.org/https://doi.org/10.1080/01919510591008344
- Afaneh, A. T., & Schreckenbach, G. (2015). Fluorescence enhancement/quenching based on metal orbital control: Computational studies of a 6-Thienyllumazine-Based Mercury Sensor. The Journal of Physical Chemistry A, 119(29), 8106–8116. https://doi.org/https://doi.org/10.1021/acs.jpca.5b04691
- Aguirre, P., García-Beltrán, O., Tapia, V., Muñoz, Y., Cassels, B. K., & Núñez, M. T. (2017). Neuroprotective effect of a new 7,8-dihydroxycoumarin-based Fe2+/Cu2+ chelator in cell and animal models of Parkinson's disease. ACS Chemical Neuroscience, 8(1), 178–185. https://doi.org/https://doi.org/10.1021/acschemneuro.6b00309
- Akram, D., Elhaty, I. A., & AlNeyadi, S. S. (2020). Synthesis and antibacterial activity of rhodanine-based azo dyes and their use as spectrophotometric chemosensor for Fe3+ ions. Chemosensors, 8(1), 16. https://doi.org/https://doi.org/10.3390/chemosensors8010016
- Anand, J. R., Rijhwani, H., Malapati, K., Kumar, P., Saikia, K., & Lakhar, M. (2013). Anticancer activity of esculetin via-modulation of Bcl-2 and NF-κB expression in benzo[a]pyrene induced lung carcinogenesis in mice. Biomedicine & Preventive Nutrition, 3(2), 107–112. https://doi.org/https://doi.org/10.1016/j.bionut.2012.11.004
- Bano, S., Mohd, A., Khan, A. A. P., & Siddiqi, K. S. (2010). Complexation and mechanism of fluorescence quenching of telmisartan with Y(III) and Nd(III). Journal of Chemical & Engineering Data, 55(12), 5759–5765. https://doi.org/https://doi.org/10.1021/je100711u
- Barceló, J., & Poschenrieder, C. (2002). Fast root growth responses, root exudates, and internal detoxification as clues to the mechanisms of aluminium toxicity and resistance: A review. Environmental and Experimental Botany, 48(1), 75–92. https://doi.org/https://doi.org/10.1016/S0098-8472(02)00013-8
- Batista, R. C., da Miranda, F. S., Pinheiro, C. B., & Lanznaster, M. (2018). An esculetin–cobalt(III) archetype for redox‐activated drug delivery platforms with hypoxic selectivity. European Journal of Inorganic Chemistry, 2018(5), 612–616. https://doi.org/https://doi.org/10.1002/ejic.201701251
- Beneduci, A., Furia, E., Russo, N., & Marino, T. (2017). Complexation behaviour of caffeic, ferulic and p-coumaric acids towards aluminium cations: A combined experimental and theoretical approach. New Journal of Chemistry, 41(12), 5182–5190. https://doi.org/https://doi.org/10.1039/C7NJ00661F
- Berthon, G. (2002). Aluminium speciation in relation to aluminium bioavailability, metabolism and toxicity. Coordination Chemistry Reviews, 228(2), 319–341. https://doi.org/https://doi.org/10.1016/S0010-8545(02)00021-8
- Catapano, M. C., Karlíčková, J., Tvrdý, V., Sharma, S., Prasad, A. K., Saso, L., Chhillar, A. K., Kuneš, J., Pour, M., Parmar, V. S., & Mladěnk, P. (2018). Mono and dihydroxy coumarin derivatives: Copper chelation and reduction ability. Journal of Trace Elements in Medicine and Biology : Organ of the Society for Minerals and Trace Elements (Gms)), 46, 88–95. https://doi.org/https://doi.org/10.1016/j.jtemb.2017.11.014
- Chilom, C. G., Craescu, C. T., & Popescu, A. I. (2006). Parameters of interaction between proteins and their specific ligands, deduced by isothermal titration calorimetry. Romanian Journal of Physics, 51, 443–457.
- Das, S., Dutta, M., & Das, D. (2013). Fluorescent probes for selective determination of trace level Al3+: Recent developments and future prospects. Analytical Methods, 5(22), 6262–6285. https://doi.org/https://doi.org/10.1039/c3ay40982a
- Dubey, S. N., & Mehrotra, R. C. (1964). Study of catechol derivatives of aluminium. Journal of Inorganic and Nuclear Chemistry, 26(9), 1543–1550. https://doi.org/https://doi.org/10.1016/0022-1902(64)80042-7
- Elmorsi, T. M., Aysha, T. S., Machalický, O., Mohamed, M. B. I., & Bedair, A. H. (2017). A dual functional colorimetric and fluorescence chemosensor based on benzo[f]fluorescein dye derivatives for copper ions and pH; kinetics and thermodynamic study. Sensors and Actuators B: Chemical, 253, 437–450. https://doi.org/https://doi.org/10.1016/j.snb.2017.06.084
- Exley, C. (2013). Human exposure to aluminium. Environmental Science Processes & Impacts, 15(10), 1807–1816. https://doi.org/https://doi.org/10.1039/c3em00374d
- Exley, C. (2016). The toxicity of aluminium in humans. Morphologie : Bulletin de L'Association Des Anatomistes, 100(329), 51–55. https://doi.org/https://doi.org/10.1016/j.morpho.2015.12.003
- Fylaktakidou, K. C., Hadjipavlou-Litina, D. J., Litinas, K. E., & Nicolaides, D. N. (2004). Natural and synthetic coumarin derivatives with anti-inflammatory/ antioxidant activities . Current Pharmaceutical Design, 10(30), 3813–3833. https://doi.org/https://doi.org/10.2174/1381612043382710
- Grazul, M., & Budzisz, E. (2009). Biological activity of metal ions complexes of chromones, coumarins and flavones. Coordination Chemistry Reviews, 253(21–22), 2588–2598. https://doi.org/https://doi.org/10.1016/j.ccr.2009.06.015
- Habashi, F. (2016). A Hundred years of the Bayer process for alumina production. In D. Donaldson & B. E. Raahauge (Eds.), Essential readings in light metals (pp. 85–93). Springer. https://doi.org/https://doi.org/10.1007/978-3-319-48176-0_12
- Harty, M., & Bearne, S. L. (2016). Measuring benzohydroxamate complexation with Mg2+, Mn2+, Co2+, and Ni2+ using isothermal titration calorimetry. Journal of Thermal Analysis and Calorimetry, 123(3), 2573–2582. https://doi.org/https://doi.org/10.1007/s10973-016-5290-4
- Hoult, J. R. S., & Paya, M. (1996). Pharmacological and biochemical actions of simple coumarins: Natural products with therapeutic potential. General Pharmacology: The Vascular System, 27(4), 713–722. https://doi.org/https://doi.org/10.1016/0306-3623(95)02112-4
- Jin, L., Wang, W., Shen, Z., Xu, J., Wang, Q., & Zhao, C. (2019). A new coumarin-based fluorescence “turn-on” sensor for Al(III) ions and its bioimaging in cell. Journal of Molecular Structure, 1197, 73–79. https://doi.org/https://doi.org/10.1016/j.molstruc.2019.07.048
- Kim, S., Kang, K., Zhang, R., Piao, M., Ko, D., Wang, Z., Chae, S., Kang, S., Lee, K., Kang, H., Kang, H., & Hyun, J. (2008). Protective effect of esculetin against oxidative stress-induced cell damage via scavenging reactive oxygen species. Acta Pharmacologica Sinica, 29(11), 1319–1326. https://doi.org/https://doi.org/10.1111/j.1745-7254.2008.00878.x
- Krewski, D., Yokel, R. A., Nieboer, E., Borchelt, D., Cohen, J., Harry, J., Kacew, S., Lindsay, J., Mahfouz, A. M., & Rondeau, V. (2007). Human health risk assessment for aluminium oxide, and aluminium hydroxide. Journal of Toxicology and Environmental Health, Part B, 10(sup1), 1–269. https://doi.org/https://doi.org/10.1080/10937400701597766
- Kruck, T. P., Cui, J.-G., Percy, M. E., & Lukiw, W. J. (2004). Molecular shuttle chelation: The use of ascorbate, desferrioxamine and Feralex-G in combination to remove nuclear bound aluminum. Cellular and Molecular Neurobiology, 24(3), 443–459. https://doi.org/https://doi.org/10.1023/B:CEMN.0000022773.70722.b2
- Lapouge, C., & Cornard, J. –P. (2007). Reaction pathways involved in the mechanism of AlIII chelation with caffeic acid: Catechol and carboxylic functions competition. Chemphyschem : A European Journal of Chemical Physics and Physical Chemistry, 8(3), 473–479. https://doi.org/https://doi.org/10.1002/cphc.200600620
- Masamoto, Y., Ando, H., Murata, Y., Shimoishi, Y., Tada, M., & Takahata, K. (2003). Mushroom tyrosinase inhibitory activity of esculetin isolated from seeds of Euphorbia lathyris L. Bioscience, Biotechnology, and Biochemistry, 67(3), 631–634. https://doi.org/https://doi.org/10.1271/bbb.67.631
- Nancollas, G. H. (1970). The thermodynamics of metal-complex and ion-pair formation. Coordination Chemistry Reviews, 5(4), 379–415. https://doi.org/https://doi.org/10.1016/S0010-8545(00)80099-5
- Palmeira-Mello, M. V., Caballero, A. B., Ribeiro, J. M., de Souza-Fagundes, E. M., Gamez, P., & Lanznaster, M. (2020). Evaluation of cobalt(III) complexes as potential hypoxia-responsive carriers of esculetin. Journal of Inorganic Biochemistry, 211, 111–211.
- Person, A. L., Moncomble, A., & Cornard, J.-P. (2014). The complexation of AlIII, PbII, and CuII metal ions by esculetin: A spectroscopic and theoretical approach. The Journal of Physical Chemistry A, 118(14), 2646–2655. https://doi.org/https://doi.org/10.1021/jp412291z
- Rabbani, G., & Choi, I. (2018). Roles of osmolytes in protein folding and aggregation in cells and their biotechnological applications. International Journal of Biological Macromolecules, 109, 483–491. https://doi.org/https://doi.org/10.1016/j.ijbiomac.2017.12.100
- Rabbani, G., Ahmad, E., Khan, M. V., Ashraf, M. T., Bhat, R., & Khan, R. H. (2015). Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): In relation to pH, chemical and thermal denaturation. RSC Advances, 5(26), 20115–20131. https://doi.org/https://doi.org/10.1039/C4RA17093H
- Rabbani, G., Ahmad, E., Zaidi, N., & Khan, R. H. (2011). pH-Dependent conformational transitions in conalbumin (ovotransferrin), a metalloproteinase from hen egg white. Cell Biochemistry and Biophysics, 61(3), 551–560. https://doi.org/https://doi.org/10.1007/s12013-011-9237-x
- Rabbani, G., Ahmad, E., Zaidi, N., Fatima, S., & Khan, R. H. (2012). pH-Induced molten globule state of Rhizopus niveus lipase is more resistant against thermal and chemical denaturation than its native state. Cell Biochemistry and Biophysics, 62(3), 487–499. https://doi.org/https://doi.org/10.1007/s12013-011-9335-9
- Rabbani, G., Kaur, J., Ahmad, E., Khan, R. H., & Jain, S. K. (2014). Structural characteristics of thermostable immunogenic outer membrane protein from Salmonella enterica serovar Typhi. Applied Microbiology and Biotechnology, 98(6), 2533–2543. https://doi.org/https://doi.org/10.1007/s00253-013-5123-3
- Rabbani, G., Khan, M. J., Ahmad, A., Maskat, M. Y., & Khan, R. H. (2014). Effect of copper oxide nanoparticles on the conformation and activityof β-galactosidase. Colloids and Surfaces B: Biointerfaces, 123, 96–105. https://doi.org/https://doi.org/10.1016/j.colsurfb.2014.08.035
- Rabbani, G., Lee, E. J., Ahmad, K., Baig, M. H., & Choi, I. (2018). Binding of tolperisone hydrochloride with human serum albumin: Effects on the conformation, thermodynamics, and activity of HSA. Molecular Pharmaceutics, 15(4), 1445–1456. https://doi.org/https://doi.org/10.1021/acs.molpharmaceut.7b00976
- Riveiro, M. E., De Kimpe, N., Moglioni, A., Vazquez, R., Monczor, F., Shayo, C., & Davio, C. (2010). Coumarins: Old compounds with novel promising therapeutic perspectives. Current Medicinal Chemistry, 17(13), 1325–1338. https://doi.org/https://doi.org/10.2174/092986710790936284
- S., Afrin, Riyazuddeen, G., Rabbani, R. H. & Khan, (2014). Spectroscopic and calorimetric studies of interaction of methimazole with human serum albumin. Journal of Luminescence, 151, 219–223. https://doi.org/https://doi.org/10.1016/j.jlumin.2014.02.028
- Sarkar, T., Bhattacharyya, A., Banerjee, S., & Hussain, A. (2020). LMCT transition-based red-light photochemotherapy using a tumour-selective ferrocenyl iron(III) coumarin conjugate. Chemical Communications (Cambridge, England)), 56(57), 7981–7984. https://doi.org/https://doi.org/10.1039/d0cc03240a
- Shinde, R. G., Khan, A. A., Kunwar, A., Tripathi, V. S., & Barik, A. (2018). Fluorescence “off” and “on” signalling of esculetin in the presence of copper and thiol: A possible implication in cellular thiol sensing. Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology, 17(9), 1197–1205. https://doi.org/https://doi.org/10.1039/c8pp00157j
- Siddiqi, M. K., Alam, P., Chaturvedi, S. K., Nusrat, S., Ajmal, M. R., Abdelhameed, A. S., & Khan, R. H. (2017). Probing the interaction of cephalosporin antibiotic-ceftazidime with human serum albumin: A biophysical investigation. International Journal of Biological Macromolecules, 105(Pt 1), 292–299. https://doi.org/https://doi.org/10.1016/j.ijbiomac.2017.07.036
- Stefanachi, A., Leonetti, F., Pisani, L., Catto, M., & Carotti, A. (2018). Coumarin: A natural, privileged and versatile scaffold for bioactive compounds. Molecules, 23, 250–284.
- Venugopala, K. N., Rashmi, V., & Odhav, B. (2013). Review on natural coumarin lead compounds for their pharmacological activity. BioMed Research International, 2013, 963248. https://doi.org/https://doi.org/10.1155/2013/963248
- Verma, P., Kunwar, A., Arai, K., Iwaoka, M., & Priyadarsini, K. I. (2016). Alkyl chain modulated cytotoxicity and antioxidant activity of bioinspired amphiphilic selenolanes. Toxicology Research, 5(2), 434–445. https://doi.org/https://doi.org/10.1039/c5tx00331h
- Wang, J., Lu, M. L., Dai, H. L., Zhang, S. P., Wang, H. X., & Wei, N. (2015). Esculetin, a coumarin derivative, exerts in vitro and in vivo antiproliferative activity against hepatocellular carcinoma by initiating a mitochondrial-dependent apoptosis pathway. Brazilian Journal of Medical and Biological Research = Revista Brasileira de Pesquisas Medicas e Biologicas, 48(3), 245–253. https://doi.org/https://doi.org/10.1590/1414-431X20144074
- Wang, X., Fan, X., Yuan, S., Jiao, W., Liu, B., Cao, J., & Jiang, W. (2017). Chlorogenic acid protects against aluminium-induced cytotoxicity through chelation and antioxidant actions in primary hippocampal neuronal cells. Food & Function, 8(8), 2924–2934. https://doi.org/https://doi.org/10.1039/c7fo00659d
- Zhang, L., Dong, S., & Zhu, L. (2007). Fluorescent dyes of the esculetin and alizarin families respond to zinc ions ratiometrically. Chemical Communications, (19), 1891–1893. https://doi.org/https://doi.org/10.1039/b618413h