European Journal of Chemistry

Molecular mechanistic vision on binding interaction of triptan drug, a serotonin (5-HT1) agonist with human serum albumin through multispectral and computational assessments

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Manjushree Makegowda
Revanasiddappa Hosakere Doddarevanna

Abstract

The triptan drug such as eletriptan in combination with hydrochloride (ETP) is a 5-HT1 receptor agonist used to treat the migraine headache. Human serum albumin (HSA), the fundamental serum protein, executes various functions, that includes transporting and binding of many ligands. HSA binding interaction with ETP is elucidated from molecular docking in composite with fluorescence (emission, 3D and synchronous), UV-vis and FT-IR spectroscopy at 296, 304 and 312 K (pH = 7.40). ETP after interaction modified the HSA secondary structure and its micro-environments. Energy transfer and thermodynamic parameters were evaluated. Various quenching and binding constants were computed for formed ETP-HSA complex. The dominant interactive forces for ETP and HSA binding are hydrogen bonds join up with van der Waals extent possibly at site III (IB). The presence of Ca2+, Co2+, Na+, Mg2+ and Fe3+ ions significantly affected binding ability of ETP towards HSA. The essentialness of this investigation is beneficial in life sciences, medicinal chemistry, pharmaceutical industry and clinical medicine.


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Makegowda, M.; Doddarevanna, R. H. Molecular Mechanistic Vision on Binding Interaction of Triptan Drug, a Serotonin (5-HT1) Agonist With Human Serum Albumin through Multispectral and Computational Assessments. Eur. J. Chem. 2020, 11, 145-155.

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References

[1]. Migraine, Wikipedia, https://en.wikipedia.org/wiki/Migraine, 2020 (Accessed 11 February 2020).

[2]. Eletriptan-hydrochloride, NPS Medicinewise, https://www.nps.org.au/australian-prescriber/articles/eletriptan-hydrochloride, 2020 (Accessed 11 February 2020).

[3]. Eletriptan, Wikipedia, https://en.wikipedia.org/wiki/Eletriptan, 2020 (Accessed 11 February 2020).

[4]. Kremer, J. M.; Wilting, J.; Janssen, L. H. Pharmacol. Rev. 1988, 40, 1-47.

[5]. Ghuman, J.; Zunszain, P. A.; Petitpas, I.; Bhattacharya, A. A.; Otagiri, M.; Curry, S. J. Mol. Biol. 2005, 353, 38-52.
https://doi.org/10.1016/j.jmb.2005.07.075

[6]. Fasano, M.; Curry, S.; Terreno, E.; Galliano, M.; Fanali, G.; Narciso, P.; Notari, S.; Ascenzi, P. IUBMB Life 2005, 57, 787-796.
https://doi.org/10.1080/15216540500404093

[7]. Zolfagharzadeh, M.; Pirouzi, M.; Asoodeh, A.; Saberi, M. R.; Chamani, J. J. Biomol. Struct. Dyn. 2013, 32, 1936-1952.
https://doi.org/10.1080/07391102.2013.843062

[8]. Kamshad, M.; Shah Talab, M.; Beigoli, S.; Sharifi, R. A.; Chamani, J. J. Biomol. Struct. Dyn. 2018, 37, 2030-2040.
https://doi.org/10.1080/07391102.2018.1475258

[9]. Manjushree, M.; Revanasiddappa, H. D. Spectrochim. Acta A 2019, 209, 264-273.

[10]. Sanei, H.; Asoodeh, A.; Hamedakbari-Tusi, S.; Chamani, J. J. Solution Chem. 2011, 40, 1905-1931.
https://doi.org/10.1007/s10953-011-9766-3

[11]. Ariga, G. G.; Naik, P. N.; Nandibewoor, S. T.; Chimatadar. S. A. J. Biomol. Struct. Dyn. 2016, 35, 3161-3175.
https://doi.org/10.1080/07391102.2016.1245159

[12]. Manjushree, M.; Revanasiddappa, H. D. Bioinorg. Chem. Appl. 2018, 6954951, 1-13.
https://doi.org/10.1155/2018/6954951

[13]. Mokaberi, P.; Reyhani, V.; Amiri-Tehranizadeh, Z.; Saberi, M. R.; Beigoli, S.; Samandar, F.; Chamani, J. New J. Chem. 2019, 43, 8132-8145.
https://doi.org/10.1039/C9NJ01048C

[14]. Sharif-Barfeh, Z.; Beigoli, S.; Marouzi, S.; Rad, A. S.; Asoodeh, A.; Chamani, J. J. Solution Chem. 2017, 46, 488-504.
https://doi.org/10.1007/s10953-017-0590-2

[15]. Manjushree, M.; Revanasiddappa, H. D. Chem. Phys. 2020, 530, 110593
https://doi.org/10.1016/j.chemphys.2019.110593

[16]. Shakibapour, N.; Dehghani Sani, F.; Beigoli, S.; Sadeghian, H.; Chamani, J. J. Biomol. Struct. Dyn. 2018, 37, 359-371.
https://doi.org/10.1080/07391102.2018.1427629

[17]. Yue, Y.; Sun, Y.; Dong, Q.; Liu, R.; Yan, X.; Zhang, Y.; Liu, J. Luminescence 2016, 31, 671-681.
https://doi.org/10.1002/bio.3010

[18]. Yue, Y.; Liu, J.; Liu, R.; Sun, Y.; Li, X.; Fan, J. Food Chem. Toxicol. 2014, 71, 244-253.
https://doi.org/10.1016/j.fct.2014.06.022

[19]. Bourassa, P.; Dubeau, S.; Maharvi, G. M.; Fauq, A. H.; Thomas, T. J.; Tajmir-Riahi, H. A. Biochimie. 2011, 93, 1089-1101.
https://doi.org/10.1016/j.biochi.2011.03.006

[20]. Abdelhameed, A. S.; Alam, P.; Khan, R. H. J. Biomol. Struct. Dyn. 2016, 159, 199-208.
https://doi.org/10.1016/j.saa.2016.01.049

[21]. Sohrabi, T.; Hosseinzadeh, M.; Beigoli, S.; Saberi, M. R.; Chamani, J. J. Mol. Liq. 2018, 256, 127-138.
https://doi.org/10.1016/j.molliq.2018.02.031

[22]. Chamani, J.; Vahedian-Movahed, H.; Saberi, M. R. J. Pharmaceut. Biomed. 2011, 55, 114-124.
https://doi.org/10.1016/j.jpba.2010.12.029

[23]. Feroz, S. R.; Mohamad, S. B.; Bujang, N.; Malek, S. N.; Tayyab, S. J. Agric. Food Chem. 2012, 60, 5899-5908.
https://doi.org/10.1021/jf301139h

[24]. Dehghani Sani, F.; Shakibapour, N.; Beigoli, S.; Sadeghian, H.; Hosainzadeh, M.; Chamani, J. J. Lumin. 2018, 203, 599-608.
https://doi.org/10.1016/j.jlumin.2018.06.083

[25]. Moosavi-Movahedi, A.; Chamani, J.; Gharanfoli, M.; Hakimelahi, G. Thermochim. Acta 2004, 409, 137-144.
https://doi.org/10.1016/S0040-6031(03)00358-7

[26]. Abdelhameed, A. S.; Alanazi, A. M.; Bakheit, A. H.; Darwish, H. W.; Ghabbour, H. A.; Darwish, I. A. Spectrochim. Acta A 2017, 171, 174-182.
https://doi.org/10.1016/j.saa.2016.08.005

[27]. Jirgensons, B. J. Biol. Chem. 1965, 240, 1064-1071.

[28]. Weiss, S. Science 1999, 283(5408), 1676-1683.
https://doi.org/10.1126/science.283.5408.1676

[29]. Roy, A. S.; Tripathy, D. R.; Chatterjee, A.; Dasgupta, S. Spectrochim. Acta A 2013, 102, 393-402.
https://doi.org/10.1016/j.saa.2012.09.053

[30]. Jacobsen, J.; Brodersen, R. J. Biol. Chem. 1983, 258, 6319-6326.

[31]. Sharifi-Rad, A.; Mehrzad, J.; Darroudi, M.; Saberi, M. R.; Chamani, J. J. Biomol. Struct. Dyn. 2020, 1-27.
https://doi.org/10.1080/07391102.2020.1724568

[32]. Guo, X. J.; Sun, X. D.; Xu, S. K. J. Mol. Struct. 2009, 931, 55-59.
https://doi.org/10.1016/j.molstruc.2007.06.035

Supporting Agencies

University Grants Commission of Basic Scientific Research (UGC-BSR) for awarding the Senior Research Fellowship (SRF) under meritorious students and Institute of Excellence (IOE), Vijnana Bhavan, Mysuru.
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