Milk caseins as useful vehicle for delivery of dipyridamole drug

References

• Abd El-Salam, M. H., & El-Shibiny, S. (2012). Formation and potential uses of milk proteins as nano delivery vehicles for nutraceuticals: A review. International Journal of Dairy Technology, 65, 13–21.10.1111/idt.2011.65.issue-1
   Web of Science ®Google Scholar
• Albani, J. R. (2007) Principles and applications of fluorescence spectroscopy (1nd ed.). Oxford: Blackwell Science, Blackwell Publishing.10.1002/9780470692059
   Google Scholar
• Barth, C. A., & Schlimme, E. (1989). Milk protein: Nutritional, clinical, functional and technological aspects. London: Springer.10.1007/978-3-642-85373-9
   Google Scholar
• Boland, M., Golding, M., & Singh, H. (2014). Food Structures, Digestion and Health (1st ed.). New Zealand: Academic press.
   Google Scholar
• Bourassa, P., Bariyanga, J., & Tajmir-Riahi, H. A. (2013). Binding sites of resveratrol, genistein, and curcumin with milk α- and β-caseins. The Journal of Physical Chemistry B, 117, 1287–1295.10.1021/jp3114557
   PubMed Web of Science ®Google Scholar
• Bourassa, P., Bekale, L., & Tajmir-Riahi, H. A. (2014). Association of lipids with milk α- and β-caseins. International Journal of Biological Macromolecules, 70, 156–166.10.1016/j.ijbiomac.2014.06.038
   PubMed Web of Science ®Google Scholar
• Bourassa, P., Chanphai, P., & Tajmir-Riahi, H. A. (2016). Folic acid delivery by serum proteins: Loading efficacy and protein morphology. Journal of Biomolecular Structure and Dynamics. Published online: 10 Nov 2016. doi:10.1080/07391102.2016.1259589
   PubMed Web of Science ®Google Scholar
• Chakraborty, A., & Basak, S. (2008). Interaction with Al and Zn induces structure formation and aggregation in natively unfolded caseins. Journal of Photochemistry and Photobiology B: Biology, 93, 36–43.10.1016/j.jphotobiol.2008.06.011
   PubMed Web of Science ®Google Scholar
• Elzoghby, A. O., El-Fotoh, W. S., & Elgindy, N. A. (2011). Casein-based formulations as promising controlled release drug delivery systems. Journal of Controlled Release, 153, 206–216.10.1016/j.jconrel.2011.02.010
   PubMed Web of Science ®Google Scholar
• Esmaili, M., Ghaffari, S. M., Moosavi-Movahedi, Z., Sadat-Atri, M., Sharifizadeh, A., Farhadi, M., Yousefi, R., … Moosavi-Movahedi, A. A. (2011). Beta casein-micelle as a nano vehicle for solubility enhancement of curcumin; food industry application. LWT- Food Science and Technology., 44, 2166–2172.10.1016/j.lwt.2011.05.023
   Web of Science ®Google Scholar
• Fox, P. F., & McSWeeny, P. L. H. (1998). Dairy Chemistry and Biochemistry (1st ed.). London: Blackie Academic & Professional.
   Google Scholar
• Gerasimov, A. V., Ziganshin, M. A., Gorbatchuk, V. V., & Usmanova, L. S. (2014). Increasing the solubility of dipyridamole using polyethylene glycols. International Journal of Pharmacy and Pharmaceutical Sciences, 6, 244–247.
   Google Scholar
• Hashizume, K., & Sato, T. (1988). Gel-forming characteristics of milk proteins. 1. Effect of heat treatment. Journal of Dairy Science, 71, 1439–1446.10.3168/jds.S0022-0302(88)79706-4
   Web of Science ®Google Scholar
• Hasni, I., Bourassa, P., Hamdani, S., Samson, G., Carpentier, R., & Tajmir-Riahi, H. A. (2011). Interaction of milk α- and β-caseins with tea polyphenols. Food Chemistry, 126, 630–639.10.1016/j.foodchem.2010.11.087
   Web of Science ®Google Scholar
• Hassouna, A., Allam, H., Awad, A., & Hassaballah, F. (2000). Standard versus low-level anticoagulation combined to low-dose dipyridamole after mitral valve replacement. Cardiovascular Surgery, 8, 491–498.10.1016/S0967-2109(00)00069-7
   PubMedGoogle Scholar
• He, Z., Xu, M., Zeng, M., Qin, F., & Chen, J. (2016). Interactions of milk α- and β-casein with malvidin-3-O-glucoside and their effects on the stability of grape skin anthocyanin extracts. Food Chemistry, 199, 314–322.10.1016/j.foodchem.2015.12.035
   PubMed Web of Science ®Google Scholar
• Jameson, G. B., Adams, J. J., & Creamer, L. K. (2002). Flexibility, functionality and hydrophobicity of bovine β-lactoglobulin. International Dairy Journal, 12, 319–329.10.1016/S0958-6946(02)00028-6
   Web of Science ®Google Scholar
• Jana, S., Dalapati, S., Ghosh, S., & Guchhait, N. (2012). Binding interaction between plasma protein bovine serum albumin and flexible charge transfer fluorophore: A spectroscopic study in combination with molecular docking and molecular dynamics simulation. Journal of Photochemistry and Photobiology A: Chemistry, 231, 19–27.10.1016/j.jphotochem.2011.12.002
   Web of Science ®Google Scholar
• Jiang, Z., Wang, L., Wu, W., & Wang, Y. (2013). Biological activities and physicochemical properties of Maillard reaction products in sugar-bovine casein peptide model systems. Food Chemistry, 141, 3837–3845.10.1016/j.foodchem.2013.06.041
   PubMed Web of Science ®Google Scholar
• Kong, D., Qin, C., Fan, P., Li, B., & Wang, J. (2015). Spectroscopic studies on interaction of BSA and Eu(III) complexes with H5ph-dtpa and H5dtpa ligands. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 140, 372–381.10.1016/j.saa.2015.01.004
   PubMed Web of Science ®Google Scholar
• Lakowicz, J. (2013). Principles of fluorescence spectroscopy (3rd ed.). New York, NY: Kluwer academic.
   Google Scholar
• Li, X., Zhou, G., Zhou, X., & Zhou, Sh (2013). The efficacy and safety of aspirin plus dipyridamole versus aspirin in secondary prevention following TIA or stroke: A meta-analysis of randomized controlled trials. Journal of the Neurological Sciences, 332, 92–96.10.1016/j.jns.2013.06.025
   PubMed Web of Science ®Google Scholar
• Livney, Y. D. (2010). Milk proteins as vehicles for bioactives. Current Opinion in Colloid & Interface Science, 15, 73–83.10.1016/j.cocis.2009.11.002
   Web of Science ®Google Scholar
• Loch, J. I., Bonarek, P., Polit, A., Świątek, S., Czub, M., Ludwikowska, M., & Lewiński, K. (2015). Conformational variability of goat β-lactoglobulin: Crystallographic and thermodynamic studies. International Journal of Biological Macromolecules, 72, 1283–1291.10.1016/j.ijbiomac.2014.10.031
   PubMed Web of Science ®Google Scholar
• Lucey, J. A. (2002). Formation and physical properties of milk protein gels. Journal of Dairy Science, 85, 281–294.10.3168/jds.S0022-0302(02)74078-2
   PubMed Web of Science ®Google Scholar
• Mehranfar, F., Bordbar, A. K., Fani, N., & Keyhanfar, M. (2013). Binding analysis for interaction of diacetylcurcumin with β-casein nanoparticles by using fluorescence spectroscopy and molecular docking calculations. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 115, 629–635.10.1016/j.saa.2013.06.062
   PubMed Web of Science ®Google Scholar
• Mehranfar, F., Bordbar, A. K., Keyhanfar, M., & Behbahani, M. (2013). Spectrofluoremetric and molecular docking study on the interaction of bisdemethoxycurcumin with bovine β-casein nanoparticles. Journal of Luminescence, 143, 687–692.10.1016/j.jlumin.2013.06.005
   Web of Science ®Google Scholar
• Messaoudi, S. E., Wouters, C. W., Swieten, H. A. V., Pickkers, P., Noyez, L., Kievit, P. C., … Rongen, G. A. (2014). Eacpt-0017-dipyridamole does not limit myocardial ischemia-reperfusion injury. A double-blind randomized placebo-controlled trial in patients undergoing elective coronary artery bypass surgery. Clinical Therapeutics, 36, e13.10.1016/j.clinthera.2014.05.052
   Google Scholar
• Michelson, A. D. (2002). Platelets (2nd ed.). Boston, MA: Elsevier.
   Google Scholar
• Moitzi, C., Portnaya, I., Glatter, O., Ramon, O., & Danino, D. (2008). Effect of temperature on self-assembly of bovine β-casein above and below isoelectric pH. Structural analysis by cryogenic-transmission electron microscopy and small-angle X-ray scattering. Langmuir, 24, 3020–3029.10.1021/la702802a
   PubMed Web of Science ®Google Scholar
• Morris, G. A. (2002). The self-assembly and structure of caseins in solution. Biotechnology and Genetic Engineering Reviews, 19, 357–376.10.1080/02648725.2002.10648034
   PubMed Web of Science ®Google Scholar
• Mote, U. S., Han, S. H., Patil, S. R., & Kolekar, G. B. (2010). Effect of temperature and pH on interaction between bovine serum albumin and cetylpyridinium bromide: Fluorescence spectroscopic approach. Journal of Luminescence, 130, 2059–2064.10.1016/j.jlumin.2010.05.027
   Web of Science ®Google Scholar
• Nakamura, T., Uchiyama, Sh, Yamazaki, M., & Iwata, M. (2007). Synergistic effect of cilostazol and dipyridamole mediated by adenosine on shear-induced platelet aggregation. Thrombosis Research, 119, 511–516.10.1016/j.thromres.2006.05.005
   PubMed Web of Science ®Google Scholar
• Petrucci, E., Mainardi, L. T., Balian, V., Ghiringhelli, S., Bianchi, A. M., Bertinelli, M., … Cerutti, S. (1996). Assessment of heart rate variability changes during dipyridamole infusion and dipyridamole induced myocardial ischemia: A time variant spectral approach1. Journal of the American College of Cardiology, 28, 924–934.10.1016/S0735-1097(96)00270-7
   PubMed Web of Science ®Google Scholar
• Portnaya, I., Cogan, U., Livney, Y.D., Ramon, O., Shimoni, K., Rosenberg, M., Danino, D. (2006). Micellization of bovine β-casein studied by isothermal titration microcalorimetry and cryogenic transmission electron microscopy. Journal of Agricultural and Food Chemistry, 54, 5555–5561.10.1021/jf060119c
   PubMed Web of Science ®Google Scholar
• Renugopalakrishnan, V., & Lewis, R. V. (2006). Bionanotechnology proteins to nanodevices (1st ed.). Dordrecht: Springer.
   Google Scholar
• Ross, D. P., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20, 3096–3102.10.1021/bi00514a017
   PubMed Web of Science ®Google Scholar
• Rungnim, C., Rungrotmongkol, T., Kungwan, N., & Hannongbua, S. (2015). Protein-protein interactions between SWCNT/chitosan/EGF and EGF receptor: A model of drug delivery system. Journal of Biomolecular Structure and Dynamics, 34, 1919–1929.
   Web of Science ®Google Scholar
• Sanyakam Dhorn, S., Agudelo, D., Tajmir-Riahi, H. A. (2016). Review on the targeted conjugation of anticancer drugs doxorubicin and tamoxifen with synthetic polymers for drug delivery. Journal of Biomolecular Structure and Dynamics. Published online: 06 Sep 2016. doi:10.1080/07391102.2016.1222971
   Web of Science ®Google Scholar
• Schwede, T., Kopp, J., Guex, N., & Peitsch, M. C. (2003). Swiss-model: An automated protein homology-modeling server. Nucleic Acids Research, 31, 3381–3385.10.1093/nar/gkg520
   PubMed Web of Science ®Google Scholar
• Singh, H. (2011). Aspects of milk-protein-stabilised emulsions. Food Hydrocolloids, 25, 1938–1944.10.1016/j.foodhyd.2011.02.022
   Web of Science ®Google Scholar
• Strauer, B. E., Heidland, U. E., Heintzen, M. P., & Schwartzkopff, B. (1996). Pharmacologic myocardial protection during percutaneous transluminal coronary angioplasty by intracoronary application of dipyridamole: Impact on hemodynamic function and left ventricular performance. Journal of the American College of Cardiology, 28, 1119–1126.10.1016/S0735-1097(96)00307-5
   PubMed Web of Science ®Google Scholar
• Tcholakova, S., Denkov, N. D., Ivanov, I. B., & Campbell, B. (2006). Coalescence stability of emulsions containing globular milk proteins. Advances in Colloid and Interface Science, 123–126, 259–293.10.1016/j.cis.2006.05.021
   PubMed Web of Science ®Google Scholar
• Thorn, D. C., Meehan, S., Sunde, M., Rekas, A., Gras, S. L., MacPhee, C. E., … Carver, J. A. (2005). Amyloid fibril formation by bovine milk қ-casein and its inhibition by the molecular chaperones αs- and β-casein. Biochemistry, 44, 17027–17036.10.1021/bi051352r
   PubMed Web of Science ®Google Scholar
• Wakure, B. S., Bhatia, N. M., & Basha Syed, H. (2015). Noninvasive cellular internalization of silver molecules by chitosan nanoneedles: A novel nano carrier. Journal of Biomolecular Structure and Dynamics, 34, 971–982.
   PubMed Web of Science ®Google Scholar
• Wang, C., Lin, W., Playa, H., Sun, Sh, Cameron, K., & Buolamwini, J. K. (2013). Dipyridamole analogs as pharmacological inhibitors of equilibrative nucleoside transporters. Identification of novel potent and selective inhibitors of the adenosine transporter function of human equilibrative nucleoside transporter 4 (hENT4). Biochemical Pharmacology, 86, 1531–1540.
   PubMed Web of Science ®Google Scholar
• Yu, D. D., Zhang, H., Ding, Q. B., Guo, H. Y., Wu, J. P., & Zhang, L. D. (2012). Spectral properties of interaction between caffeic acid and milk protein and the change in antioxidant capacity. Spectroscopy Spectral Analysis, 32, 1061–1067.
   Web of Science ®Google Scholar
• Zhang, X. P., Hou, Y. H., Wang, L., Zhang, Y Zh, & Liu, Y. (2013). Exploring the mechanism of interaction between sulindac and human serum albumin: Spectroscopic and molecular modeling methods. Journal of Luminescence, 138, 8–14.10.1016/j.jlumin.2012.12.059
   Web of Science ®Google Scholar
• Zhang, G., & Ma, Y. (2013). Mechanistic and conformational studies on the interaction of food dye amaranth with human serum albumin by multispectroscopic methods. Food Chemistry, 136, 442–449.10.1016/j.foodchem.2012.09.026
   PubMed Web of Science ®Google Scholar