Molecular interaction studies of P3CL on bovine serum albumin through biophysical approach

References

• Ali, I., Nadeem Lone, M., An Al-Othman, Z., Al-Warthan, A., & Marsin Sanagi, M. (2015). Heterocyclic scaffolds: Centrality in anticancer drug development. Current Drug Targets, 16(7), 711–734. https://doi.org/10.2174/1389450116666150309115922
   PubMed Web of Science ®Google Scholar
• Alsaif, N. A.,Wani, T. A.,Bakheit, A. H., &Zargar, S. (2020). Multi-spectroscopic investigation, molecular docking and molecular dynamic simulation of competitive interactions between flavonoids (quercetin and rutin) and sorafenib for binding to human serum albumin. International Journal of Biological Macromolecules, 165(Pt B), 2451–2461. https://doi.org/10.1016/j.ijbiomac.2020.10.098 33122058
   PubMed Web of Science ®Google Scholar
• Banerjee, A., Mohanty, M., Lima, S., Samanta, R., Garribba, E., Sasamori, T., & Dinda, R. (2020). Synthesis, structure and characterization of new dithiocarbazate-based mixed ligand oxidovanadium(IV) complexes: DNA/HSA interaction, cytotoxic activity and DFT studies. New Journal of Chemistry, 44(26), 10946–10963. https://doi.org/10.1039/D0NJ01246G
   Web of Science ®Google Scholar
• 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: The Journal of Biological and Chemical Luminescence, 28(2), 149–155. https://doi.org/10.1002/bio.2354
   PubMed Web of Science ®Google Scholar
• Callis, P. R. (2014). Binding phenomena and fluorescence quenching. II: Photophysics of aromatic residues and dependence of fluorescence spectra on protein conformation. Journal of Molecular Structure, 1077, 22–29. https://doi.org/10.1016/j.molstruc.2014.04.051
   Web of Science ®Google Scholar
• Das, P., Chaudhari, S. K., Das, A., Kundu, S., & Saha, C. (2019). Interaction of flavonols with human serum albumin: A biophysical study showing structure–activity relationship and enhancement when coated on silver nanoparticles. Journal of Biomolecular Structure & Dynamics, 37(6), 1414–1426. https://doi.org/10.1080/07391102.2018.1462732
   PubMed Web of Science ®Google Scholar
• Dehkordi, M. F., Farhadian, S., Abdolvand, M., Soureshjani, E. H., Rahmani, B., & Darzi, S. (2021). Deciphering the DNA-binding affinity, cytotoxicity and apoptosis induce as the anticancer mechanism of Bavachinin: An experimental and computational investigation. Journal of Molecular Liquids, 341, 117373. https://doi.org/10.1016/j.molliq.2021.117373
   Web of Science ®Google Scholar
• Eslami-Farsani, R., Shareghi, B., Farhadian, S., & Momeni, L. (2021). Experimental and theoretical investigations on the interaction of glucose molecules with myoglobin in the aqueous solution using theoretical and experimental methods. Journal of Biomolecular Structure & Dynamics, 39(17), 6384–6395. https://doi.org/10.1080/07391102.2020.1798283
   PubMed Web of Science ®Google Scholar
• Farajzadeh-Dehkordi, N., Farhadian, S., Zahraei, Z., Gholamian-Dehkordi, N., & Shareghi, B. (2021). Interaction of reactive Red195 with human serum albumin: Determination of the binding mechanism and binding site by spectroscopic and molecular modeling methods. Journal of Molecular Liquids, 327, 114835. https://doi.org/10.1016/j.molliq.2020.114835
   Web of Science ®Google Scholar
• Raeessi-Babaheydari,E., Farhadian, S., &Shareghi, B. ( 2021). Evaluation of interaction betweencitrus flavonoid, naringenin, and pepsin using spectroscopic analysis anddocking simulation. Journal of Molecular Liquids, 339, 116763. https://doi.org/10.1016/j.molliq.2021.116763
   Web of Science ®Google Scholar
• Ferreira, L. G., Dos Santos, R. N., Oliva, G., & Andricopulo, A. D. (2015). Molecular docking and structure-based drug design strategies. Molecules, 20(7), 13384–13421. https://doi.org/10.3390/molecules200713384
   PubMed Web of Science ®Google Scholar
• Ghosh, K., Rathi, S., & Arora, D. (2016). Fluorescence spectral studies on interaction of fluorescent probes with bovine serum albumin (BSA). Journal of Luminescence, 175, 135–140. https://doi.org/10.1016/j.jlumin.2016.01.029
   Web of Science ®Google Scholar
• Gnanaselvan, S., Yadav, S. A., & Manoharan, S. P. (2023). Structure-based virtual screening of anti-breast cancer compounds from Artemisia absinthium – Insights through molecular docking, pharmacokinetics, and molecular dynamic simulations. Journal of Biomolecular Structure & Dynamics, 1–19. https://doi.org/10.1080/07391102.2023.2212805
   PubMed Web of Science ®Google Scholar
• Goncharova, I., Orlov, S., & Urbanová, M. (2013). The location of the high-and low-affinity bilirubin-binding sites on serum albumin: Ligand-competition analysis investigated by circular dichroism. Biophysical Chemistry, 180-181, 55–65. https://doi.org/10.1016/j.bpc.2013.06.004
   PubMed Web of Science ®Google Scholar
• Hashemi-Shahraki, F., Shareghi, B., & Farhadian, S. (2021). Characterizing the binding affinity and molecular interplay between quinoline yellow and pepsin. Journal of Molecular Liquids, 341, 117317. https://doi.org/10.1016/j.molliq.2021.117317
   Web of Science ®Google Scholar
• Hirata, K., Kawai, A., Chuang, V. T. G., Sakurama, K., Nishi, K., Yamasaki, K., & Otagiri, M. (2022). Effects of myristate on the induced circular dichroism spectra of aripiprazole bound to human serum albumin: A structural–chemical investigation. ACS Omega, 7(5), 4413–4419. https://doi.org/10.1021/acsomega.1c06220
   PubMed Web of Science ®Google Scholar
• Jairajpuri, D. S., Fatima, S., & Jairajpuri, Z. S. (2015). Glycation induced physicochemical changes in low-density lipoprotein and its role in promoting cholesterol accumulation in macrophages along with antiglycation effect of aminoguanidine. Advances in Biological Chemistry, 5(5), 203–214. https://doi.org/10.4236/abc.2015.55017
   Google Scholar
• Jattinagoudar, L., Meti, M., Nandibewoor, S., & Chimatadar, S. (2016). Evaluation of the binding interaction between bovine serum albumin and dimethyl fumarate, an anti-inflammatory drug by multispectroscopic methods. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 156, 164–171. https://doi.org/10.1016/j.saa.2015.11.026
   PubMed Web of Science ®Google Scholar
• Jorgensen, W. L. (2004). The many roles of computation in drug discovery. Science, 303(5665), 1813–1818. https://doi.org/10.1126/science.1096361
   PubMed Web of Science ®Google Scholar
• Kandagal, P. B., Ashoka, S., Seetharamappa, J., Shaikh, S. M. T., Jadegoud, Y., & Ijare, O. B. (2006). Study of the interaction of an anticancer drug with human and bovine serum albumin: Spectroscopic approach. Journal of Pharmaceutical and Biomedical Analysis, 41(2), 393–399. https://doi.org/10.1016/j.jpba.2005.11.037
   PubMed Web of Science ®Google Scholar
• Lakowicz, J. R., & Fu, Y. (2009). Modification of single molecule fluorescence near metallic nanostructures. Laser & Photonics Reviews, 3(1–2), 221–232. https://doi.org/10.1002/lpor.200810035
   PubMed Web of Science ®Google Scholar
• Li, G., Cheng, Y., Han, C., Song, C., Huang, N., & Du, Y. (2022). Pyrazole-containing pharmaceuticals: Target, pharmacological activity, and their SAR studies. RSC Medicinal Chemistry, 13(11), 1300–1321. https://doi.org/10.1039/d2md00206j
   PubMedGoogle Scholar
• Liu, E. H., Qi, L. W., & Li, P. (2010). Structural relationship and binding mechanisms of five flavonoids with bovine serum albumin. Molecules, 15(12), 9092–9103. https://doi.org/10.3390/molecules15129092
   PubMed Web of Science ®Google Scholar
• Li, J., & Yao, P. (2009). Self-assembly of ibuprofen and bovine serum albumin-dextran conjugates leading to effective loading of the drug. Langmuir: The ACS Journal of Surfaces and Colloids, 25(11), 6385–6391. https://doi.org/10.1021/la804288u
   PubMed Web of Science ®Google Scholar
• Mermer, A. (2021). The importance of rhodanine scaffold in medicinal chemistry: A comprehensive overview. Mini-Reviews in Medicinal Chemistry, 21(6), 738–789. https://doi.org/10.2174/1389557521666201217144954
   PubMed Web of Science ®Google Scholar
• Mohammadi, M., Shareghi, B., Farhadian, S., & Saboury, A. A. (2021). The effect of sorbitol on the structure and activity of carboxypeptidase A: Insights from a spectroscopic and computational approach. Journal of Molecular Liquids, 330, 115710. https://doi.org/10.1016/j.molliq.2021.115710
   Web of Science ®Google Scholar
• Moman, R. N., Gupta, N., & Varacallo, M. (2022). Physiology, albumin. StatPearls.
   Google Scholar
• Mousavi, S. M., Zarei, M., Hashemi, S. A., Babapoor, A., & Amani, A. M. (2019). A conceptual review of rhodanine: Current applications of antiviral drugs, anticancer and antimicrobial activities. Artificial Cells, Nanomedicine, and Biotechnology, 47(1), 1132–1148. https://doi.org/10.1080/21691401.2019.1573824
   PubMed Web of Science ®Google Scholar
• Naik, P. N., Chimatadar, S. A., & Nandibewoor, S. T. (2010). Interaction between a potent corticosteroid drug–dexamethasone with bovine serum albumin and human serum albumin: A fluorescence quenching and Fourier transformation infrared spectroscopy study. Journal of Photochemistry and Photobiology. B, Biology, 100(3), 147–159. https://doi.org/10.1016/j.jphotobiol.2010.05.014
   PubMed Web of Science ®Google Scholar
• Naseri, A., Hosseini, S., Rasoulzadeh, F., Rashidi, M. R., Zakery, M., & Khayamian, T. (2015). Interaction of norfloxacin with bovine serum albumin studied by different spectrometric methods; displacement studies, molecular modeling and chemometrics approaches. Journal of Luminescence, 157, 104–112. https://doi.org/10.1016/j.jlumin.2014.08.031
   Web of Science ®Google Scholar
• Pal, S., Saha, C., Hossain, M., Dey, S. K., & Kumar, G. S. (2012). Influence of galloyl moiety in interaction of epicatechin with bovine serum albumin: A spectroscopic and thermodynamic characterization. PLoS One, 7(8), e43321. https://doi.org/10.1371/journal.pone.0043321
   PubMed Web of Science ®Google Scholar
• Palleria, C., Di Paolo, A., Giofrè, C., Caglioti, C., Leuzzi, G., Siniscalchi, A., De Sarro, G., & Gallelli, L. (2013). Pharmacokinetic drug-drug interaction and their implication in clinical management. Journal of Research in Medical Sciences, 18(7), 601–610.
   PubMed Web of Science ®Google Scholar
• Phan, H. T., Bartelt-Hunt, S., Rodenhausen, K. B., Schubert, M., & Bartz, J. C. (2015). Investigation of bovine serum albumin (BSA) attachment onto self-assembled monolayers (SAMs) using combinatorial quartz crystal microbalance with dissipation (QCM-D) and spectroscopic ellipsometry (SE). PLoS One, 10(10), e0141282. https://doi.org/10.1371/journal.pone.0141282
   PubMed Web of Science ®Google Scholar
• Qi, X., Xu, D., Zhu, J., Wang, S., Peng, J., Gao, W., & Cao, Y. (2021). Studying the interaction mechanism between bovine serum albumin and lutein dipalmitate: Multi-spectroscopic and molecular docking techniques. Food Hydrocolloids. 113, 106513. https://doi.org/10.1016/j.foodhyd.2020.106513
   Web of Science ®Google Scholar
• Rahman, A. J., Kaur, L., Pathak, M., Singh, A., Verma, P., Singhal, R., Kumar, V., & Ojha, H. (2021). Spectroscopic studies of binding interactions of 2-chloroethylphenyl sulphide with bovine serum albumin. Journal of Molecular Liquids, 340, 117144. https://doi.org/10.1016/j.molliq.2021.117144
   Web of Science ®Google Scholar
• Rahman, A. J., Sharma, D., Kumar, D., Pathak, M., Singh, A., Kumar, V., Chawla, R., & Ojha, H. (2021). Spectroscopic and molecular modelling study of binding mechanism of bovine serum albumin with phosmet. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 244, 118803. https://doi.org/10.1016/j.saa.2020.118803
   PubMed Web of Science ®Google Scholar
• Sadeghi-Kaji, S., Shareghi, B., Saboury, A. A., & Farhadian, S. (2019). Investigation on the structure and function of porcine pancreatic elastase (PPE) under the influence of putrescine: A spectroscopy and molecular simulation study. Journal of Molecular Liquids, 289, 111115. https://doi.org/10.1016/j.molliq.2019.111115
   Web of Science ®Google Scholar
• Saeedi, M., Hadjiakhondi, A., Mohammad Nabavi, S., & Manayi, A. (2017). Heterocyclic compounds: Effective α-amylase and α-glucosidase inhibitors. Current Topics in Medicinal Chemistry, 17(4), 428–440. https://doi.org/10.2174/1568026616666160824104655
   PubMed Web of Science ®Google Scholar
• Sampath, S., Yadav, S. A., Meti, M., Kaveri, S., Subban, R., & Subramanyam, R. (2024). Elucidation of binding mechanism of rhodanine derivative P4OC on bovine serum albumin. Journal of Biomolecular Structure & Dynamics, 42(1), 475–482. https://doi.org/10.1080/07391102.2023.2194001
   PubMedGoogle Scholar
• Shahabadi, N., & Fili, S. M. (2014). Molecular modeling and multi spectroscopic studies of the interaction of mesalamine with bovine serum albumin. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 118, 422–429. https://doi.org/10.1016/j.saa.2013.08.110
   PubMed Web of Science ®Google Scholar
• Subramanyam, R.,Gollapudi, A.,Bonigala, P.,Chinnaboina, M., &Amooru, D. G. (2009). Betulinic acid binding to human serum albumin: a study of protein conformation and binding affinity. Journal of Photochemistry and Photobiology. B, Biology, 94(1), 8–12. 10.1016/j.jphotobiol.2008.09.002 18945624
   PubMed Web of Science ®Google Scholar
• Truskewycz, A., Yin, H., Halberg, N., Lai, D. T. H., Ball, A. S., Truong, V. K., Rybicka, A. M., & Cole, I. (2022). Carbon dot therapeutic platforms: Administration, distribution, metabolism, excretion, toxicity, and therapeutic potential. Small, 18(16), e2106342. https://doi.org/10.1002/smll.202106342
   PubMed Web of Science ®Google Scholar
• Vinod, S. M., Murugan Sreedevi, S., Krishnan, A., Ravichandran, K., Karthikeyan, P., Kotteswaran, B., & Rajendran, K. (2023). Complexity of the role of various site-specific and selective Sudlow binding site drugs in the energetics and stability of the acridinedione dye–bovine serum albumin complex: A molecular docking approach. ACS Omega, 8(6), 5634–5654. https://doi.org/10.1021/acsomega.2c07111
   PubMed Web of Science ®Google Scholar
• Vlasiou, M. C., & Pafiti, K. S. (2020). Spectroscopic evaluation of Zn (II) complexes with drug analogues: Interactions with BSA and the pH effect on the drug-Zn (II) system. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 241, 118641. https://doi.org/10.1016/j.saa.2020.118641
   PubMed Web of Science ®Google Scholar
• Wani, T. A., AlRabiah, H., Bakheit, A. H., Kalam, M. A., & Zargar, S. (2017). Study of binding interaction of rivaroxaban with bovine serum albumin using multi-spectroscopic and molecular docking approach. Chemistry Central Journal, 11(1), 134. https://doi.org/10.1186/s13065-017-0366-1
   PubMedGoogle Scholar
• Wani, T. A., Bakheit, A. H., Zargar, S., & Alamery, S. (2022). Mechanistic competitive binding interaction study between olmutinib and colchicine with model transport protein using spectroscopic and computer simulation approaches. Journal of Photochemistry and Photobiology A: Chemistry, 426, 113794. https://doi.org/10.1016/j.jphotochem.2022.113794
   Web of Science ®Google Scholar
• Yadav, S. A., Faruck, L. H., Subramanium, R., Surendren, L. K., & Bakshi, H. (2021). Screening and assessment of molecular mechanistic actions of 5-hydroxy-1-methylpiperidin-2-one against free radicals, lung cancer cell line (A549), and binding properties on bovine serum albumin. Future Journal of Pharmaceutical Sciences, 7(1), 1–11. https://doi.org/10.1186/s43094-021-00277-5
   Web of Science ®Google Scholar
• Yadav, S. A., Yeggoni, D. P., Devadasu, E., & Subramanyam, R. (2018). Molecular binding mechanism of 5-hydroxy-1-methylpiperidin-2-one with human serum albumin. Journal of Biomolecular Structure & Dynamics, 36(3), 810–817. https://doi.org/10.1080/07391102.2017.1300106
   PubMed Web of Science ®Google Scholar
• Yadollahi, E., Shareghi, B., & Farhadian, S. (2022). Noncovalent interactions between Quinoline yellow and trypsin: In vitro and in silico methods. Journal of Molecular Liquids, 353, 118826. https://doi.org/10.1016/j.molliq.2022.118826
   Web of Science ®Google Scholar
• Yeggoni, D. P., Rachamallu, A., & Subramanyam, R. (2016). Protein stability, conformational change and binding mechanism of human serum albumin upon binding of embelin and its role in disease control. Journal of Photochemistry and Photobiology. B, Biology, 160, 248–259. https://doi.org/10.1016/j.jphotobiol.2016.04.012
   PubMed Web of Science ®Google Scholar
• Zhang, Y. Z., Zhou, B., Zhang, X. P., Huang, P., Li, C. H., & Liu, Y. (2009). Interaction of malachite green with bovine serum albumin: Determination of the binding mechanism and binding site by spectroscopic methods. Journal of Hazardous Materials, 163(2–3), 1345–1352. https://doi.org/10.1016/j.jhazmat.2008.07.132
   PubMed Web of Science ®Google Scholar