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Research Articles

Modulation of the structural and functional properties of α1-antitrypsin by interaction with flavonoid luteolin

ORCID Icon & ORCID Icon
Pages 7884-7891 | Received 28 Jul 2022, Accepted 15 Sep 2022, Published online: 02 Oct 2022

References

  • Ali, M. S., Rehman, M. T., Al-Lohedan, H., & AlAjmi, M. F. (2022). Spectroscopic and molecular docking investigation on the interaction of cumin components with plasma protein: Assessment of the comparative interactions of aldehyde and alcohol with human serum albumin. International Journal of Molecular Sciences, 23(8), 4078. https://doi.org/10.3390/ijms23084078
  • Azouz, N. P., Klingler, A. M., Callahan, V., Akhrymuk, I. V., Elez, K., Raich, L., Henry, B. M., Benoit, J. L., Benoit, S. W., Noé, F., Kehn-Hall, K., & Rothenberg, M. E. (2021). Alpha 1 antitrypsin is an inhibitor of the SARS-CoV-2-priming protease TMPRSS2. Pathogens & Immunity, 6(1), 55–74. https://doi.org/10.20411/pai.v6i1.408.
  • Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N., & Bourne, P. E. (2000). The protein data bank. Nucleic Acids Research, 28(1), 235–242. https://doi.org/10.1093/nar/28.1.235
  • BIOVIA. (2021). Dassault Systèmes [Discovery Studio]. Dassault Systèmes.
  • Boerema, D. J., An, B., Gandhi, R. P., Papineau, R., Regnier, E., Wilder, A., Molitor, A., Tang, A. P., & Kee, S. M. (2017). Biochemical comparison of four commercially available human α1-proteinase inhibitors for treatment of α1-antitrypsin deficiency. Biologicals: Journal of the International Association of Biological Standardization, 50, 63–72. https://doi.org/10.1016/j.biologicals.2017.08.010
  • Bouriche, H., Salavei, P., Lessig, J., & Arnhold, J. (2007). Differential effects of flavonols on inactivation of α1-antitrypsin induced by hypohalous acids and the myeloperoxidase–hydrogen peroxide–halide system. Archives of Biochemistry and Biophysics, 459(1), 137–142. https://doi.org/10.1016/j.abb.2006.10.030
  • Brantly, M., Nukiwa, T., & Crystal, R. G. (1988). Molecular basis of alpha-1-antitrypsin deficiency. The American Journal of Medicine, 84(6A), 13–31. https://doi.org/10.1016/0002-9343(88)90154-4
  • Cazacu, N., Popescu, A. I., & Chilom, C. G. (2022). Spectroscopic and molecular docking approach of the interaction of vitamins with human serum transferrin. Chemical Physics, 555, 111459. https://doi.org/10.1016/j.chemphys.2022.111459
  • Celej, M. S., Montich, G. G., & Fidelio, G. D. (2003). Protein stability induced by ligand binding correlates with changes in protein flexibility. Protein Science, 12(7), 1496–1506. https://doi.org/10.1110/ps.0240003
  • Chang, Y. P., Mahadeva, R., Chang, W. W., Lin, S. C., & Chu, Y. H. (2009). Small-molecule peptides inhibit Z alpha1-antitrypsin polymerization. Journal of Cellular and Molecular Medicine. 13(8B), 2304–2316. https://doi.org/10.1111/j.1582-4934.2008.00608.x
  • Dallakyan, S., & Olson, A. J. (2015). Small-molecule library screening by docking with PyRx. Methods in Molecular Biology (Clifton, N.J.), 1263, 243–250. https://doi.org/10.1007/978-1-4939-2269-7_19
  • Ekeowa, U. I., Gooptu, B., Belorgey, D., Hägglöf, P., Karlsson-Li, S., Miranda, E., Pérez, J., MacLeod, I., Kroger, H., Marciniak, S. J., Crowther, D. C., & Lomas, D. A. (2009). Alpha1-antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies. Clinical Science (London, England: 1979), 116(12), 837–850. https://doi.org/10.1042/CS20080484
  • Frenzel, E., Wrenger, S., Brügger, B., Salipalli, S., Immenschuh, S., Aggarwal, N., Lichtinghagen, R., Mahadeva, R., Marcondes, A. M. Q., Dinarello, C. A., Welte, T., & Janciauskiene, S. (2015). α1-antitrypsin combines with plasma fatty acids and induces angiopoietin-like protein 4 expression. The Journal of Immunology, 195(8), 3605–3616. https://doi.org/10.4049/jimmunol.1500740
  • Gao, W., Zhao, J., Kim, H., Xu, S., Chen, M., Bai, X., Toba, H., Cho, H.-R., Zhang, H., Keshavjeel, S., & Liu, M. (2014). α1-Antitrypsin inhibits ischemia reperfusion-induced lung injury by reducing inflammatory response and cell death. The Journal of Heart and Lung Transplantation: The Official Publication of the International Society for Heart Transplantation, 33(3), 309–315. https://doi.org/10.1016/j.healun.2013.10.031
  • George, V. C., Kumar, D. R. N., Suresh, P. K., Kumar, S., & Kumar, R. A. (2013). Comparative studies to evaluate relative in vitro potency of luteolin in inducing cell cycle arrest and apoptosis in HaCaT and A375 cells. Asian Pacific Journal of Cancer Prevention, 14(2), 631–637. https://doi.org/10.7314/apjcp.2013.14.2.631
  • Glaser, C. B., & Karic, L. (1978). Spectral studies on two genetic forms of the human serum proteinase inhibitor, alpha-1-antitrypsin. International Journal of Peptide and Protein Research, 12(5), 284–292. https://doi.org/10.1111/j.1399-3011.1978.tb02899.x
  • Horinaka, M., Yoshida, T., Shiraishi, T., Nakata, S., Wakada, M., Nakanishi, R., Nishino, H., Matsui, H., & Sakai, T. (2005). Luteolin induces apoptosis via death receptor 5 upregulation in human malignant tumor cells. Oncogene, 24(48), 7180–7189. https://doi.org/10.1038/sj.onc.1208874
  • https://pubchem.ncbi.nlm.nih.gov/compound/Luteolin
  • https://www.rcsb.org/structure/1kct
  • Jakimiuk, K., Gesek, J., Atanasov, A. G., & Tomczyk, M. (2021). Flavonoids as inhibitors of human neutrophil elastase. Journal of Enzyme Inhibition and Medicinal Chemistry, 36(1), 1016–1028. https://doi.org/10.1080/14756366.2021.1927006
  • Kim, S., Chen, J., Cheng, T., Gindulyte, A., He, J., He, S., Li, Q., Shoemaker, B. A., Thiessen, P. A., Yu, B., Zaslavsky, L., Zhang, J., & Bolton, E. E. (2019). PubChem 2019 update: Improved access to chemical data. Nucleic Acids Research, 47(D1), D1102–D1109. https://doi.org/10.1093/nar/gky1033
  • Koloczek, H., Banbula, A., Salvesen, G. S., & Potempa, J. (1996). Serpin α-1 proteinase inhibitor probed by intrinsic tryptophan fluorescence spectroscopy. Protein Science: A Publication of the Protein Society, 5(11), 2226–2235. https://doi.org/10.1002/pro.5560051109
  • Kwon, K. S., Kim, J., Shin, H. S., & Yu, M. H. (1994). Single amino acid substitutions of a1-antitrypsin that confer enhancement in thermal stability. Journal of Biological Chemistry, 269(13), 9627–9631. https://doi.org/10.1016/S0021-9258(17)36927-2
  • Lakowicz, R. (2007). Principles of fluorescence spectroscopy (443–475). Plenum Press.
  • Law, R. H. P., Zhang, Q., McGowan, S., Buckle, A. M., Silverman, G. A., Wong, W., Rosado, C. J., Langendorf, C. G., Pike, R. N., Bird, P. I., & Whisstock, J. C. (2006). An overview of the serpin superfamily. Genome Biology, 7(5), 216. https://doi.org/10.1186/gb-2006-7-5-216
  • Lin, Y., Shi, R., Wang, X., & Shen, H.-M. (2008). Luteolin, a flavonoid with potentials for cancer prevention and therapy. Current Cancer Drug Targets, 8(7), 634–646. https://doi.org/10.2174/156800908786241050
  • Liu, L., Ma, H., Yang, N., Tang, Y., Guo, J., Tao, W., & Duan, J. (2010). A series of natural flavonoids as thrombin inhibitors: Structure-activity relationships. Thrombosis Research, 126(5), e365-78–e378. https://doi.org/10.1016/j.thromres.2010.08.006
  • López-Lázaro, M. (2009). Distribution and biological activities of the flavonoid luteolin. Mini Reviews in Medicinal Chemistry, 9(1), 31–59. https://doi.org/10.2174/138955709787001712
  • Mansuri, M.L., Parihar. P., Solanki , I., Parihar, M.S. (2014). Flavonoids in modulation of cell survival signalling pathways. Genes Nutr., 9(3), 400. https://doi.org/10.1007/s12263-014-0400-z.
  • Matsuo, M., Sasaki, N., Saga, K., & Kaneko, T. (2005). Cytotoxicity of flavonoids toward cultured normal human cells. Biological & Pharmaceutical Bulletin, 28(2), 253–259. https://doi.org/10.1248/bpb.28.253
  • Mozzicafreddo, M., Cuccioloni, M., Bonfili, L., Eleuteri, A. M., Fioretti, E., & Angeletti, M. (2008). Antiplasmin activity of natural occurring polyphenols. Biochimica et Biophysica Acta, 1784(7–8), 995–1001. https://doi.org/10.1016/j.bbapap.2008.03.016
  • Niklas, J., Nonnenmacher, Y., Rose, T., Sandig, V., & Heinzle, E. (2012). Quercetin treatment changes fluxes in the primary metabolism and increases culture longevity and recombinant α1-antitrypsin production in human AGE1.HN cells. Applied Microbiology and Biotechnology, 94(1), 57–67. https://doi.org/10.1007/s00253-011-3811-4
  • Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004). UCSF Chimera—A visualization system for exploratory research and analysis. Journal of Computational Chemistry, 25(13), 1605–1612. https://doi.org/10.1002/jcc.20084
  • Sandu, N., Chilom, C. G., & Popescu, A. I. (2021). Structural and molecular aspects of flavonoids as ligands for serum transferrin. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 254, 119600. https://doi.org/10.1016/j.saa.2021.119600
  • Seelinger, G., Merfort, I., Wölfle, U., & Schempp, C. M. (2008). Anti-carcinogenic effects of the flavonoid luteolin. Molecules (Basel, Switzerland), 13(10), 2628–2651. https://doi.org/10.3390/molecules13102628
  • Song, H. K., Lee, K. N., Kwon, K. S., Yu, M. H., & Suh, S. W. (1995). Crystal structure of an uncleaved α1-antitrypsin reveals the conformation of its inhibitory reactive loop. FEBS Letters, 377(2), 150–154. https://doi.org/10.1016/0014-5793(95)01331-8
  • Teckman, J. H., An, J. K., Blomenkamp, K., Schmidt, B., & Perlmutter, D. (2004). Mitochondrial autophagy and injury in the liver in alpha 1-antitrypsin deficiency. American Journal of Physiology. Gastrointestinal and Liver Physiology, 286(5), G851–G862. https://doi.org/10.1152/ajpgi.00175.2003
  • Tew, D. J., & Bottomley, S. P. (2001). Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state. Journal of Molecular Biology, 313(5), 1161–1169. https://doi.org/10.1006/jmbi.2001.5104
  • Tian, Z., Tian, L., Shi, M., Zhao, S., Guo, S., Luo, W., Wang, C., & Tian, Z. (2020). Investigation of the interaction of a polyamine-modified flavonoid with bovine serum albumin (BSA) by spectroscopic methods and molecular simulation. Journal of Photochemistry and Photobiology B: Biology, 209, 111917. https://doi.org/10.1016/j.jphotobiol.2020.111917
  • Trott, O., & Olson, A. J. (2010). AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry, 31(2), 455–461. https://doi.org/10.1002/jcc.21334
  • Wang, T., Zeng, L.-H., & Li, D.-L. (2017). A review on the methods for correcting the fluorescence inner-filter effect of fluorescence spectrum. Applied Spectroscopy Reviews, 52(10), 883–908. https://doi.org/10.1080/05704928.2017.1345758
  • Xie, F., Lang, Q., Zhou, M., Zhang, H., Zhang, Z., Zhang, Y., Wan, B., Huang, Q., & Yu, L. (2012). The dietary flavonoid luteolin inhibits Aurora B kinase activity and blocks proliferation of cancer cells. European Journal of Pharmaceutical Sciences: Official Journal of the European Federation for Pharmaceutical Sciences, 46(5), 388–396. https://doi.org/10.1016/j.ejps.2012.03.002
  • Xue, G., Gong, L., Yuan, C., Xu, M., Wang, X., Jiang, L., & Huang, M. (2017). A structural mechanism of flavonoids in inhibiting serine proteases. Food & Function, 8(7), 2437–2443. 8. https://doi.org/10.1039/C6FO01825D
  • YaĞar, H., Özcan, H. M., & Mehmet, O. (2021). A new electrochemical impedance biosensor based on aromatic thiol for alpha-1 antitrypsin determination. Turkish Journal of Chemistry, 45(1), 104–118. https://doi.org/10.3906/kim-2007-6

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