262
Views
5
CrossRef citations to date
0
Altmetric
Research Articles

Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis

, , , , , , & show all
Pages 79-90 | Received 29 Nov 2019, Accepted 06 Dec 2019, Published online: 03 Feb 2020

References

  • Ahmed-Ouameur, A., Diamantoglou, S., Sedaghat-Herati, M. R., Nafisi, S., Carpentier, R., & Tajmir-Riahi, H. A. (2006). An overview of drug binding to human serum albumin: Protein folding and unfolding. Cell Biochemistry and Biophysics, 45, 203. doi:10.1385/CBB:45:2:203
  • Akdogan, Y., Reichenwallner, J., & Hinderberger, D. (2012). Evidence for water-tuned structural differences in proteins: An approach emphasizing variations in local hydrophilicity. PLoS One, 7(9), e45681. doi:10.1371/journal.pone.0045681
  • Arnold, K., Bordoli, A. K., Kopp, L., & Schwede, T. (2006). A web-based environment for protein structure homology modeling. Bioinformatics, 22(2), 195–201. doi:10.1093/bioinformatics/bti770
  • Beauchemin, R., N'soukpoé-Kossi, C. N., Thomas, T. J., Thomas, T., Carpentier, R., & Tajmir-Riahi, H. A. (2007). Polyamine analogues bind human serum albumin. Biomacromolecules, 8(10), 3177–3183. doi:10.1021/bm700697a
  • Belgorosky, D., Langle, Y., Prack Mc Cormick, B., Colombo, L., Sandes, E., & Eiján, A. M. (2014). Inhibition of nitric oxide is a good therapeutic target for bladder tumors that express iNOS. Nitric Oxide, 36, 11–18. doi:10.1016/j.niox.2013.10.010
  • Bekale, L., Agudelo, D., & Tajmir-Riahi, H. A. (2015). Effect of polymer molecular weight on chitosan-protein interaction. Colloids and Surfaces B: Biointerfaces, 125, 309–317. doi:10.1016/j.colsurfb.2014.11.037
  • Bekale, L., Chanphai, P., Sanyakamdhorn, S., Agudelo, D., & Tajmir-Riahi, H. A. (2014). Microscopic and thermodynamic analysis of PEG-lactoglobulin interaction. RSC Advances, 4(59), 31084–31093. doi:10.1039/C4RA03303E
  • Bérubé, G., & Reyes-Moreno, C. (2017). Aminobenzoic acid derivatives for use as anti-inflammatory agents, anti-metastatic agents and/or anticancer agents. WO2017/, 177316, A1.
  • Bose, A. (2016). Interaction of tea polyphenols with serum albumins: A fluorescence spectroscopic analysis. Journal of Luminescense., 169, 220–226. doi:10.1016/j.jlumin.2015.09.018
  • Bourassa, P., Hasni, I., & Tajmir-Riahi, H. A. (2011). Folic acid complexes with human and bovine serum albumins. Food Chemistry, 129(3), 1148–1155. doi:10.1016/j.foodchem.2011.05.094
  • Byler, D. M., & Susi, H. (1986). Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 25(3), 469–487. doi:10.1002/bip.360250307
  • Carmichael, J., DeGraff, W. G., Gazdar, A. F., Minna, J. D., & Mitchell, J. B. (1987). Evaluation of a tetrazolium-based semiautomated colorimetric assay: Assessment of chemosensitivity testing. Cancer Research, 47(4), 936–942.
  • Chandra, S., Dietrich, S., Lang, H., & Bahadur, D. (2011). Dendrimer–doxorubicin conjugate for enhanced therapeutic effects for cancer. Journal of Materials Chemistry, 21(15), 5729–5737. doi:10.1039/c0jm04198j
  • Chanphai, P., Ouellette, V., Bérubé, G., & Tajmir-Riahi, H. A. (2018). Conjugation of testo and testo-Pt(II) with serum proteins: Loading efficacy and protein conformation. International Journal of Biological Macromolecules, 118, 1112–1119. doi:10.1016/j.ijbiomac.2018.06.186
  • Chanphai, P., Vesper, A. R., Bekale, L., Bérubé, G., & Tajmir-Riahi, H. A. (2015a). Encapsulation of testosterone and its aliphatic and aromatic dimers by milk beta-lactoglobulin. International Journal of Biological Macromolecules, 76, 153–160. doi:10.1016/j.ijbiomac.2015.02.028
  • Chanphai, P., Vesper, A. R., Bekale, L., Bérubé, G., & Tajmir-Riahi, H. A. (2015b). Transporting testosterone and its dimers by serum proteins. Journal of Photochemistry and Photobiology B: Biology, 153, 173–183. doi:10.1016/j.jphotobiol.2015.09.008
  • Collini, M., D'Alfonso, L., & Baldini, G. (2000). New insights on β-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay. Protein Science, 9(10), 1968–1974. doi:10.1110/ps.9.10.1968
  • Colotta, F., Allavena, P., Sica, A., Garlanda, C. A., & Mantovani, A. (2009). Cancer-related inflammation, the seventh hallmark of cancer: Links to genetic instability. Carcinogenesis, 30(7), 1073–1081. doi:10.1093/carcin/bgp127
  • Dai, X., Yan, J., Fu, X., Pan, Q., Sun, D., Xu, Y., … Geng, M. (2017). Aspirin inhibits cancer metastasis and angiogenesis via targeting heparanase. Clinical Cancer Research, 23(20), 6267–6278. doi:10.1158/1078-0432.CCR-17-0242
  • Dallagi, A., Girouard, J., Hamelin-Morrissette, J., Dadzie, R., Laurent, L., Vaillancourt, C., … Reyes-Moreno, C. (2015). The activating effect of IFN-gamma on monocytes/macrophages is regulated by the LIF-trophoblast-IL-10 axis via Stat1 inhibition and Stat3 activation. Cellular & Molecular Immunology, 12(3), 326–341. doi:10.1038/cmi.2014.50
  • Dousseau, F., Therrien, M., & Pezolet, M. (1989). On the spectral subtraction of water from the FT-IR spectra of aqueous solutions of proteins. Applied Spectroscopy, 43(3), 538–542. doi:10.1366/0003702894202814
  • Dufresne, M., Dumas, G., Asselin, E., Carrier, C., Pouliot, M., & Reyes-Moreno, C. (2011). Pro-inflammatory type-1 and anti-inflammatory type-2 macrophages differentially modulate cell survival and invasion of human bladder carcinoma T24 cells. Molecular Immunology, 48(12–13), 1556–1567. doi:10.1016/j.molimm.2011.04.022
  • Dumas, G., Dufresne, M., Asselin, E., Girouard, J., Carrier, C., & Reyes-Moreno, C. (2013). CD40 pathway activation reveals dual function for macrophages in human endometrial cancer cell survival and invasion. Cancer Immunology, Immunotherapy, 62(2), 273–283. doi:10.1007/s00262-012-1333-2
  • Elsadek, B., & Kratz, F. (2012). Impact of albumin on drug delivery-new applications on the horizon . Journal of Controlled Release : Official Journal of the Controlled Release Society, 157(1), 4–28. doi:10.1016/j.jconrel.2011.09.069
  • Essemine, J., Hasni, I., Carpentier, R., Thomas, T. J., & Tajmir-Riahi, H. A. (2011). Binding of biogenic and synthetic polyamines to β-lactoglobulin. International Journal of Biological Macromolecules, 49(2), 201–211. doi:10.1016/j.ijbiomac.2011.04.016
  • Fabris, V. T., Lodillinsky, C., Pampena, M. B., Belgorosky, D., Lanari, C., & Eiján, A. M. (2012). Cytogenetic characterization of the murine bladder cancer model MB49 and the derived invasive line MB49-I. Cancer Genetics, 205(4), 168–176. doi:10.1016/j.cancergen.2012.02.002
  • Ghuman, J., Zunszain, P. A., Petitpas, I., Bhattacharya, A. A., Otagiri, M., & Curry, S. (2005). Structural basis of the drug-binding specificity of human serum albumin. Journal of Molecular Biology, 353(1), 38–52. doi:10.1016/j.jmb.2005.07.075
  • Gokara, M., Kimavath, G. B., Podile, A. R., & Subramanyam, R. (2015). Differential interactions and structural stability of chitosan oligomers with human serum albumin and α-1-glycoprotein. Journal of Biomolecular Structure and Dynamics, 33(1), 196–210. doi:10.1080/07391102.2013.868321
  • Grdadolnik, J. (2003). Saturation effects in FTIR spectroscopy: Intensity of amide I and amide II bands in protein spectra. Acta Chimica Slovenica, 50, 777–788.
  • Hamelin-Morrissette, J., Cloutier, S., Girouard, J., Belgorosky, D., Eijan, A.-M., Legault, J., … Reyes-Moreno, C. (2015). Identification of an anti-Inflammatory derivative with anti-cancer potential: The impact of each of its structural components on inflammatory responses in macrophages and bladder cancer cells. European Journal of Medicinal Chemistry, 96, 259–268. doi:10.1016/j.ejmech.2015.04.026
  • Hasni, I., Bourassa, P., & Tajmir-Riahi, H. A. (2011). Binding of cationic lipids to milk β-lactoglobulin. The Journal of Physical Chemistry. B, 115(20), 6683–6690. doi:10.1021/jp200045h
  • Jameson, G. B., Adams, J. J., & Creamer, L. K. (2002). Flexibility, functionality and hydrophobicity of bovine β-lactoglobulin. International Dairy Journal, 12(4), 319–329. doi:10.1016/S0958-6946(02)00028-6
  • Kratochwil, N. A., Huber, W., Müller, F., Kansy, M., & Gerber, P. R. (2002). Predicting plasma protein binding of drugs: A new approach. Biochemical Pharmacology, 64(9), 1355–1374. doi:10.1016/S0006-2952(02)01074-2
  • Kratz, F. (2008). Albumin as a drug carrier: Design of prodrugs, drug conjugates and nanoparticles. Journal of Controlled Release, 132(3), 171–183. doi:10.1016/j.jconrel.2008.05.010
  • Kratz, F., & Elsadek, B. (2012). Clinical impact of serum proteins on drug delivery. Journal of Controlled Release, 161(2), 429–445. doi:10.1016/j.jconrel.2011.11.028
  • Krimm, S., & Bandekar, J. (1986). Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Advances in Protein Chemistry, 38, 181–364. doi:10.1016/s0065-3233(08)60528-8
  • Leduc, K., Bourassa, V., Asselin, E., Leclerc, P., Lafond, J., & Reyes-Moreno, C. (2012). Leukemia inhibitory factor regulates differentiation of trophoblast-like BeWo cells through the activation of JAK/STAT and MAPK3/1 MAP kinase-signaling pathways. Biology of Reproduction, 86, 1–10.
  • Loch, J. I., Bonarek, P., Polit, A., Świątek, S., Czub, M., Ludwikowska, M., & Lewiński, K. (2015). Conformational variability of goat beta-lactoglobulin: Crystallographic and thermodynamic studies. International Journal of Biological Macromolecules, 72, 1283–1291. doi:10.1016/j.ijbiomac.2014.10.031
  • Nakamura, K., & Smyth, M. J. (2017). Targeting cancer-related inflammation in the era of immunotherapy. Immunology and Cell Biology, 95(4), 325–332.
  • Nerusu, A., Reddy, P. S., Ramachary, D. B., & Subramanyam, R. (2017). Unraveling the stability of plasma proteins upon interaction of synthesized androstenedione and its derivatives—A biophysical and computational approach. ACS Omega, 2(10), 6514–6524. doi:10.1021/acsomega.7b00577
  • Painter, L., Harding, M. M., & Beeby, P. J. (1998). Synthesis and interaction with human serum albumin of the first 3,18-disub-stituted derivative of bilirubin. Journal of the Chemical Society, Perkin Transactions 1, 18, 3041–3044. doi:10.1039/a803429j
  • Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20(11), 3096–3102. doi:10.1021/bi00514a017
  • Rost, B. (1999). Twilight zone of protein sequence alignment. Protein Engineering, Design and Selection, 12(2), 85–94. doi:10.1093/protein/12.2.85
  • Sugio, S., Kashima, A., Mochizuki, S., Noda, M., & Kobayashi, K. (1999). Crystal structure of human serum albumin at 2.5 Å resolution. Protein Engineering, Design and Selection, 12(6), 439–444.
  • Sui, X., Lei, L., Chen, L., Xie, T., & Li, X. (2017). Inflammatory microenvironment in the initiation and progression of bladder cancer. Oncotarget, 8(54), 93279–93294. doi:10.18632/oncotarget.21565
  • Tian, J., Liu, J., Hu, Z., & Chen, X. (2005). Binding of the scutellarin to albumin using tryptophan fluorescence quenching, CD and FT-IR spectra. American Journal of Immunology, 1, 21–23. doi:10.3844/ajisp.2005.21.23
  • Yang, F., Zhang, Y., & Liang, H. (2014). Interactive association of drugs binding to human serum albumin. International Journal of Molecular Sciences, 15(3), 3580–3595. doi:10.3390/ijms15033580
  • Yeggoni, D. P., Gokara, M., Manidhar, D. M., Rachamallu, A., Nakka, S., Reddy, C. S., & Subramanyam, R. (2014). Binding and molecular dynamics studies of 7-hydroxycoumarin derivatives with human serum albumin and its pharmacological importance. Molecular Pharmaceutics, 11(4), 1117–1131. doi:10.1021/mp500051f
  • Zhong, W., Wang, Y., Yu, J. S., Liang, Y., Ni, K., & Tu, S. (2004). The interaction of human serum albumin with a novel antidiabetic agent-SU-118. Journal of Pharmaceutical Sciences, 93(4), 1039–1046. doi:10.1002/jps.20005
  • Zhu, Z., Shen, Z., & Xu, C. (2012). Inflammatory pathways as promising targets to increase chemotherapy response in bladder cancer. Mediators of Inflammation, 2012, 528690. doi:10.1155/2012/528690

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.