208
Views
1
CrossRef citations to date
0
Altmetric
Research Articles

Molecular interactions and binding dynamics of Alpelisib with serum albumins: insights from multi-spectroscopic techniques and molecular docking

&
Pages 2127-2143 | Received 24 Nov 2022, Accepted 10 Apr 2023, Published online: 26 Apr 2023

References

  • Ali, M. S., & Al-Lohedan, H. A. (2019). Experimental and computational investigation on the molecular interactions of safranal with bovine serum albumin: Binding and anti- amyloid genic efficacy of ligand. Journal of Molecular Liquids, 278, 385–393. https://doi.org/10.1016/j.molliq.2019.01.034
  • Bray, F., Ferlay, J., Soerjomataram, I., Siegel, R. L., Torre, L. A., & Jemal, A. (2018). Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA: A Cancer Journal for Clinicians, 68(6), 394–424. https://doi.org/10.3322/caac.21492
  • Carter, D. C., & Ho, J. X. (1994). Structure of serum albumin. Advances in Protein Chemistry, 45, 153–203. https://doi.org/10.1016/s0065-3233(08)60640-3
  • Chakraborty, B., Roy, A. S., Dasgupta, S., & Basu, S. (2010). Magnetic field effect corroborated with docking study to explore photoinduced electron transfer in drug–protein interaction. The Journal of Physical Chemistry. A, 114(51), 13313–13325. https://doi.org/10.1021/jp109604a
  • Cheng, Z. J., Zhao, H. M., Xu, Q. Y., & Liu, R. (2013). Investigation of the interaction between indigotin and two serum albumins by spectroscopic approaches. Journal of Pharmaceutical Analysis, 3(4), 257–269. https://doi.org/10.1016/j.jpha.2013.01.004
  • El Gammal, R. N., Elmansi, H., El-Emam, A. A., Belal, F., & Hammouda, M. E. A. (2022). Exploring the molecular interaction of mebendazole with bovine serum albumin using multi-spectroscopic approaches and molecular docking. Scientific Reports, 12(1), 11582. https://doi.org/10.1038/s41598-022-15696-4
  • Fatemeh, R., & Mohammad, H. F. (2022). Comprehensive investigation of binding of some polycyclic aromatic hydrocarbons with bovine serum albumin: Spectroscopic and molecular docking studies. Bioorganic Chemistry, 120, 105656. https://doi.org/10.1016/j.bioorg.2022.105656
  • Garneau, A. P., Haydock, L., Tremblay, L. E., & Isenring, P. (2021). Somatic non-cancerous PIK3CA-related overgrowth syndrome treated with Alpelisib in North America. Journal of Molecular Medicine (Berlin, Germany), 99(3), 311–313. https://doi.org/10.1007/s00109-020-02030-6
  • Gasteiger, J., & Marsili, M. (1980). Iterative partial equalization of orbital electronegativity-a rapid access to atomic charges. Tetrahedron, 36(22), 3219–3228. https://doi.org/10.1016/0040-4020(80)80168-2
  • Haris, P. I., & Chapman, D. (1995). The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers, 37(4), 251–263. https://doi.org/10.1002/bip.360370404
  • Hashempour, S., Shahabadi, N., Adewoye, A., Murphy, B., Rouse, C., Salvatore, B. A., Stratton, C., & Mahdavian, E. (2020). Binding studies of AICAR and human serum albumin by spectroscopic, theoretical, and computational methodologies. Molecules (Basel, Switzerland), 25(22), 5410. https://doi.org/10.3390/molecules25225410
  • Jahanban-Esfahlan, A., Dastmalchi, S., & Davaran, S. (2016). A simple improved desolvation method for the rapid preparation of albumin nanoparticles. International Journal of Biological Macromolecules, 91, 703–709. https://doi.org/10.1016/j.ijbiomac.2016.05.032
  • Jahanban-Esfahlan, A., Davaran, S., & Dastmalchi, S. (2022). Preparation and antiproliferative activity evaluation of Juglone-loaded BSA nanoparticles. Advanced Pharmaceutical Bulletin, 12(4), 818–827. https://doi.org/10.34172/apb.2022.087
  • Jahanban-Esfahlan, A., Davaran, S., Moosavi-Movahedi, A., & Dastmalchi, S. (2017). Investigating the interaction of juglone (5-hydroxy-1, 4-naphthoquinone) with serum albumins using spectroscopic and in silico methods. Journal of the Iranian Chemical Society, 14(7), 1527–1540. https://doi.org/10.1007/s13738-017-1094-0
  • Jahanban-Esfahlan, A., Ostadrahimi, A., Jahanban-Esfahlan, R., Roufegarinejad, L., Tabibiazar, M., & Amarowicz, R. (2019). Recent developments in the detection of bovine serum albumin. International Journal of Biological Macromolecules, 138, 602–617. https://doi.org/10.1016/j.ijbiomac.2019.07.096
  • Jahanban-Esfahlan, A., & Panahi-Azar, V. (2016). Interaction of glutathione with bovine serum albumin: Spectroscopy and molecular docking. Food Chemistry, 202, 426–431. https://doi.org/10.1016/j.foodchem.2016.02.026
  • Jahanban-Esfahlan, A., Panahi-Azar, V., & Sajedi, S. (2015). Spectroscopic and molecular docking studies on the interaction between N-acetyl cysteine and bovine serum albumin. Biopolymers, 103(11), 638–645. https://doi.org/10.1002/bip.22697
  • Jahanban-Esfahlan, A., Roufegarinejad, L., Jahanban-Esfahlan, R., Tabibiazar, M., & Amarowicz, R. (2020). Latest developments in the detection and separation of bovine serum albumin using molecularly imprinted polymers. Talanta, 207, 120317. https://doi.org/10.1016/j.talanta.2019.120317
  • Jahanban-Esfahlan, A., Roufegarinejad, L., Tabibiazar, M., Lorenzo Jose, M., & Amarowicz, R. (2021). Exploring the interactions between caffeic acid and human serum albumin using spectroscopic and molecular docking techniques. Polish Journal of Food and Nutrition Sciences, 71, 69–77. https://doi.org/10.31883/pjfns/133203
  • Juric, D., Janku, F., Rodón, J., Burris, H. A., Mayer, I. A., Schuler, M., Seggewiss-Bernhardt, R., Gil-Martin, M., Middleton, M. R., Baselga, J., Bootle, D., Demanse, D., Blumenstein, L., Schumacher, K., Huang, A., Quadt, C., & Rugo, H. S. (2019). Alpelisib plus fulvestrant in PIK3CA-altered and PIK3CA-wild-type estrogen receptor-positive advanced breast cancer: A Phase 1b clinical trial. JAMA Oncology, 5(2), e184475. https://doi.org/10.1001/jamaoncol.2018.4475
  • Juric, D., Rodon, J., Tabernero, J., Janku, F., Burris, H. A., Schellens, J. H. M., Middleton, M. R., Berlin, J., Schuler, M., Gil-Martin, M., Rugo, H. S., Seggewiss-Bernhardt, R., Huang, A., Bootle, D., Demanse, D., Blumenstein, L., Coughlin, C., Quadt, C., & Baselga, J. (2018). Phosphatidylinositol 3-kinase alpha-selective inhibition with Alpelisib (BYL719) in PIK3CA altered solid tumors: Results from the first-in-human study. Journal of Clinical Oncology, 36(13), 1291–1299. https://doi.org/10.1200/JCO.2017.72.7107
  • Kara, G., & Gabriel, G. (2013). Quenching mechanism of human serum albumin fluorescence by gangleron. Proceedings of the Yerevan State University, 6–10.
  • Katrahalli, U., Yallur, B. C., Manjunatha, D. H., & Krishna, P. M. (2019). BSA interaction and DNA cleavage studies of anti-bacterial benzothiazol-2-yl-malonaldehyde. Journal of Molecular Structure, 1196, 96–104. https://doi.org/10.1016/j.molstruc.2019.06.062
  • Kaur, L., Rahman, A., Singh, A., Pathak, M., Datta, A., Singhal, R., & Ojha, H. (2022). Binding studies for the interaction between hazardous organophosphorus compound phosmet and lysozyme: Spectroscopic and In-silico analyses. Journal of Molecular Liquids, 355, 118954. https://doi.org/10.1016/j.saa.2020.118803
  • Kelly, S. M., Jess, T. J., & Price, N. C. (2005). How to study proteins by circular dichroism. Biochimica et Biophysica Acta, 1751(2), 119–139. https://doi.org/10.1016/j.bbapap.2005.06.005
  • Kim, K. J., Kim, J. W., Sung, J. H., Suh, K. J., Lee, J. Y., Kim, S. H., Lee, J. O., Kim, J. W., Kim, Y. J., Kim, J. H., Bang, S. M., Lee, J. S., Kim, H. K., & Lee, K. W. (2020). PI3K-targeting strategy using Alpelisib to enhance the antitumor effect of paclitaxel in human gastric cancer. Scientific Reports, 10(1), 12308.23 https://doi.org/10.1038/s41598-020-68998-w
  • Kirstein, A. S., Augustin, A., Penke, M., Cea, M., Körner, A., Kiess, W., & Garten, A. (2019). The Novel phosphatidylinositol-3-kinase (PI3K) inhibitor Alpelisib effectively inhibits growth of PTEN-haploinsufficient lipoma cells. Cancers, 11(10), 1586. https://doi.org/10.3390/cancers11101586
  • Kragh-Hansen, U., Chuang, V. T. G., & Otagiri, M. (2002). Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biological & Pharmaceutical Bulletin, 25(6), 695–704. https://doi.org/10.1248/bpb.25.695
  • Lankowicz, J. R. (2006). Principles of fluorescence spectroscopy (3rd ed.). Springer Science + Business Media.
  • Lin, S. Y., Wei, Y. S., Li, M. J., & Wang, S. L. (2004). Effect of ethanol or/and captopril on the secondary structure of human serum albumin before and after protein binding. European Journal of Pharmaceutics and Biopharmaceutics, 57(3), 457–464. https://doi.org/10.1016/j.ejpb.2004.02.005
  • López Gutiérrez, J. C., Lizarraga, R., Delgado, C., Martínez Urrutia, M. J., Díaz, M., Miguel, M., & Triana, P. (2019). Alpelisib treatment for genital vascular malformation in a patient with congenital lipomatous overgrowth, vascular malformations, epidermal nevi, and spinal/skeletal anomalies and/or scoliosis (CLOVES) syndrome. Journal of Pediatric and Adolescent Gynecology, 32(6), 648–650. https://doi.org/10.1016/j.jpag.2019.07.003
  • Markham, A. (2019). Alpelisib: First global approval. Drugs, 79(11), 1249–1253. https://doi.org/10.1007/s40265-019-01161-6
  • Mayer, I., A., Abramson, V. G., Formisano, L., Balko, J. M., Estrada, M. V., Sanders, M. E., Juric, D., Solit, D., Berger, M. F., Won, H. H., Li, Y., Cantley, L. C., Winer, E., & Arteaga, C. L. (2017). A phase Ib study of Alpelisib (BYL719), a PI3Kα-specific inhibitor, with letrozole in ER+/HER2- metastatic breast cancer. Clinical Cancer Research, 23(1), 26–34. https://doi.org/10.1158/1078-0432.CCR-16-0134
  • Morris, G. M., Goodsell, D. S., & Halliday, R. S. (2007). AutoDock, Version 4.0.1., The Scripps Research Institute, La Jolla.
  • Naik, R., & Jaldappagari, S. (2019). Spectral and computational attributes: Binding of a potent anticancer agent, dasatinib to a transport protein. Journal of Molecular Liquids, 293, 111492. https://doi.org/10.1016/j.molliq.2019.111492
  • Olson, R. E., & Christ, D. D. (1996). Plasma protein binding to drugs. Annual Reports in Medicinal Chemistry, 3, 327–336. https://doi.org/10.1016/S0065-7743(08)60472-8
  • Patar, M., Jalan, A., & Moyon, N. S. (2022). A fluorescence and molecular docking study on the interaction of 4’-Hydroxychalcone with bovine serum albumin and human serum albumin. Asian Journal of Chemistry, 34(7), 1711–1722. https://doi.org/10.14233/ajchem.2022.23663
  • Pawar, S. K., Naik, R. S., & Seetharamappa, J. (2017). Exploring the binding of two potent anticancer drugs bosutinib and imatinib mesylate with bovine serum albumin: Spectroscopic and molecular dynamic simulation studies. Analytical and Bioanalytical Chemistry, 409(27), 6325–6335. https://doi.org/10.1007/s00216-017-0565-6
  • Pereira, B., Chin, S.-F., Rueda, O. M., Vollan, H.-K M., Provenzano, E., Bardwell, H. A., Pugh, M., Jones, L., Russell, R., Sammut, S.-J., Tsui, D. W. Y., Liu, B., Dawson, S.-J., Abraham, J., Northen, H., Peden, J. F., Mukherjee, A., Turashvili, G., Green, A. R., … Caldas, C. (2016). The somatic mutation profiles of 2,433 breast cancers refines their genomic and transcriptomic landscapes. Nature Communications, 7, 11479. https://doi.org/10.1038/ncomms11479
  • Peters, T. (1984). Serum albumin. Advances in Protein Chemistry, 37, 161–124. https://doi.org/10.1016/S0065-3233(08)60065-0
  • 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
  • Rao, H., Qi, W., Su, R., He, Z., & Peng, X. (2020). Mechanistic and conformational studies on the interaction of human serum albumin with rhodamine B by NMR, spectroscopic and molecular modelling methods. Journal of Molecular Liquids, 316, 113889. https://doi.org/10.1016/j.molliq.2020.113889
  • Raza, M., Ahmad, A., Yue, F., Khan, Z., Jiang, Y., Wei, Y., Raza, S., He, W. W., Khan, F. U., & Qipeng, Y. (2017). Biophysical and molecular docking approaches for the investigation of biomolecular interactions between amphotericin B and bovine serum albumin. Journal of Photochemistry and Photobiology. B, Biology, 170, 6–15. https://doi.org/10.1016/j.jphotobiol.2017.03.014
  • Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20(11), 3096–3102. https://doi.org/10.1021/bi00514a017
  • Roufegarinejad, L., Amarowicz, R., & Jahanban-Esfahlan, A. (2019). Characterizing the interaction between pyrogallol and human serum albumin by spectroscopic and molecular docking methods. Journal of Biomolecular Structure & Dynamics, 37(11), 2766–2775. https://doi.org/10.1080/07391102.2018.1496854
  • Roufegarinejad, L., Jahanban‐Esfahlan, A., Sajed‐Amin, S., Panahi‐Azar, V., & Tabibiazar, M. (2018). Molecular interactions of thymol with bovine serum albumin: Spectroscopic and molecular docking studies. Journal of Molecular Recognition: JMR, 31(7), e2704. https://doi.org/10.1002/jmr.2704
  • Sarmah, S., Pahari, S., Belwal, V. K., Jana, M., & Roy, A. S. (2020). Elucidation of molecular interaction of bioactive flavonoid luteolin with human serum albumin and its glycated analogue using multi-spectroscopic and computational studies. Journal of Molecular Liquids, 318, 114147. https://doi.org/10.1016/j.molliq.2020.114147
  • Shen, G. F., Liu, T. T., Wang, Q., Jiang, M., & Shi, J. H. (2015). Spectroscopic and molecular docking studies of binding interaction of gefitinib, lapatinib and sunitinib with bovine serum albumin (BSA). Journal of Photochemistry and Photobiology. B, Biology, 153, 380–390. https://doi.org/10.1016/j.jphotobiol.2015.10.023
  • Shi, Y., Liu, H., Xu, M., Li, Z., Xie, G., Huang, L., & Zeng, Z. (2012). Spectroscopic studies on the interaction between an anticancer drug ampelopsin and bovine serum albumin. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 87, 251–257. https://doi.org/10.1016/j.saa.2011.11.048
  • Shi, J. H., Pan, D. q., Jiang, M., Liu, T. T., & Wang, Q. (2016). Binding interaction of ramipril with bovine serum albumin (BSA): Insights from multi-spectroscopy and molecular docking methods. Journal of Photochemistry and Photobiology. B, Biology, 164, 103–111. https://doi.org/10.1016/j.jphotobiol.2016.09.025
  • Siddiqui, S., Ameen, F., Ur Rehman, S., Sarwar, T., & Tabish, M. (2021). Studying the interaction of drug/ligand with serum albumin. Journal of Molecular Liquids, 336, 116200. https://doi.org/10.1016/j.molliq.2021.116200
  • Singh, N., Kumar, N., Rathee, G., Sood, D., Singh, A., Tomar, V., Dass, S. K., & Chandra, R. (2020). Privileged Scaffold Chalcone: Synthesis, characterization and its mechanistic interaction studies with BSA employing spectroscopic and chemoinformatics approaches. ACS Omega, 5(5), 2267–2279. https://doi.org/10.1021/acsomega.9b03479
  • Society AC. (2020, September 10). Breast cancer facts and figures 2019–2020. Retrieved 2020, October 8, from https://www.cancer.org/content/dam/cancer-org/research/cancer-facts-and-statistics/breast-cancer-facts-andfigures/breast-cancer-facts-and-figures-2019-2020.pdf.
  • Sood, D., Kumar, N., Rathee, G., Singh, A., Tomar, V., & Chandra, R. (2018). Mechanistic interaction study of bromo-noscapine with bovine serum albumin employing spectroscopic and chemoinformatics approaches. Scientific Reports, 8(1), 1–11. https://doi.org/10.1038/s41598-018-35384-6
  • Sudlow, G., Birkett, D. J., & Wade, D. N. (1975). Characterization of 2 specific drug binding-sites on human serum albumin. Molecular Pharmacology, 11, 824–832.
  • Suryawanshi, V. D., Walekar, L. S., Gore, A. H., Anbhule, P. V., & Kolekar, G. B. (2016). Spectroscopic analysis on the binding interaction of biologically active pyrimidine derivative with bovine serum albumin. Journal of Pharmaceutical Analysis, 6(1), 56–63. https://doi.org/10.1016/j.jpha.2015.07.001
  • Tayyab, S., Izzudin, M. M., Kabir, M. Z., Feroz, S. R., Tee, W. V., Mohamad, S. B., & Alias, Z. (2016). Binding of an anticancer drug, axitinib to human serum albumin: Fluorescence quenching and molecular docking study. Journal of Photochemistry and Photobiology. B, Biology, 162, 386–394. https://doi.org/10.1016/j.jphotobiol.2016.06.049
  • Tiwari, R., Mahasenan, K., Pavlovicz, R., Li, C., & Tjarks, W. (2009). Carborane clusters in computational drug design: A comparative docking evaluation using AutoDock, FlexX, Glide, and Surflex. Journal of Chemical Information and Modeling, 49(6), 1581–1589. https://doi.org/10.1021/ci900031y
  • Xu, H., Chen, K., Shang, R., Chen, X., Zhang, Y., Song, X., Evert, M., Zhong, S., Li, B., Calvisi, D. F., & Chen, X. (2021). Alpelisib combination treatment as novel targeted therapy against hepatocellular carcinoma. Cell Death & Disease, 12(10), 920. https://doi.org/10.1038/s41419-021-04206-5
  • Yang, J., Nie, J., Ma, X., Wei, Y., Peng, Y., & Wei, X. (2019). Targeting PI3K in cancer: Mechanisms and advances in clinical trials. Molecular Cancer, 18(1), 26. https://doi.org/10.1186/s12943-019-0954-x
  • Zhang, X., Li, L., Xu, Z., Liang, Z., Su, J., Huang, J., & Li, B. (2013). Investigation of the interaction of naringin palmitate with bovine serum albumin: Spectroscopic analysis and molecular docking. PLoS One, 8(3), e59106. https://doi.org/10.1371/journal.pone.0059106
  • Zhang, G., Wang, A., Jiang, T., & Guo, J. (2008). Interaction of the irisflorentin with bovine serum albumin: A fluorescence quenching study. Journal of Molecular Structure, 891(1–3), 93–97. https://doi.org/10.1016/j.molstruc.2008.03.002
  • Zhao, Y., & Truhlar, D. G. (2008). Density functionals with broad applicability in chemistry. Accounts of Chemical Research, 41(2), 157–167. https://doi.org/10.1021/ar700111a

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.