Abstract
In the present study, we fabricated epigallocatechin-3-gallate (EGCG) loaded albumin nanoparticles (Alb-NP-EGCG) to enhance bioavailability and improve pharmacokinetic parameters of EGCG. The physicochemical properties of the Alb-NP-EGCG were studied using scanning electron microscopy, differential scanning calorimetry, powder X-ray diffraction and in vitro release studies. Characterization of Alb-NP-EGCG indicated the formation of spherical nanoparticles with no drug and excipient interaction. Alb-NP-EGCG showed a high drug loading capacity of 92%. Further, in vitro study showed a sustained release of EGCG from Alb-NP-EGCG over a period of 48 h. Mathematical modeling and release kinetics indicated that the Alb-NP-EGCG followed zero order kinetic and EGCG was released via fickian diffusion method. In vivo bioavailability and distribution of Alb-NP-EGCG showed an enhanced plasma concentration of EGCG with 1.5 fold increase along with prolonged T1/2 of 15.6 h in the system when compared with the free EGCG. All this study demonstrated the fabrication of EGCG loaded albumin nanoparticles which favored the slow and sustained release of EGCG with improved pharmacokinetics and bioavailability thereby prolonging the action of EGCG. Additional acute and sub-acute toxicity test of the Alb-NP-EGCG demonstrated the safety of the Alb-NP-EGCG. Therefore, the Alb-NP-EGCG could be a promising drug delivery system for EGCG.
Similar content being viewed by others
References
Arora D, Kumar A, Gupta P et al (2017) Preparation, characterization and cytotoxic evaluation of bovine serum albumin nanoparticles encapsulating 5-methylmellein: a secondary metabolite isolated from Xylaria psidii. Bioorg Med Chem Lett 27:5126–5130. https://doi.org/10.1016/j.bmcl.2017.10.064
Bae KH, Chung HJ, Park TG (2011) Nanomaterials for cancer therapy and imaging. Mol Cells 31:295–302. https://doi.org/10.1007/s10059-011-0051-5
Barbu E, Molnàr É, Tsibouklis J, Górecki DC (2009) The potential for nanoparticle-based drug delivery to the brain: overcoming the blood–brain barrier. Expert Opin Drug Deliv 6:553–566. https://doi.org/10.1517/17425240902939143
Bhushan B, Dubey P, Kumar SU et al (2015) Bionanotherapeutics: niclosamide encapsulated albumin nanoparticles as a novel drug delivery system for cancer therapy. RSC Adv 5:12078–12086. https://doi.org/10.1039/c4ra15233f
Bronze-Uhle ES, Costa BC, Ximenes VF, Lisboa-Filho PN (2017) Synthetic nanoparticles of bovine serum albumin with entrapped salicylic acid. Nanotechnol Sci Appl 10:11–21. https://doi.org/10.2147/NSA.S117018
Casa DM, Scariot DB, Khalil NM et al (2018) Bovine serum albumin nanoparticles containing amphotericin B were effective in treating murine cutaneous leishmaniasis and reduced the drug toxicity. Exp Parasitol. https://doi.org/10.1016/j.exppara.2018.07.003
Chen L, Lee M, Li HE et al (1997) Absorption, distribution, elimination of tea polyphenols in rats. Drug Metab Dispos 25:1045–1050
Chinedu E, Arome D, Ameh FS (2013) A new method for determining acute toxicity in animal models. Toxicol Int 20:224–226. https://doi.org/10.4103/0971-6580.121674
Costa P, Lobo JMS (2001) Modelling and comparison of dissolution profiles. Eur J Pharm Sci 13:123–133. https://doi.org/10.1016/S0928-0987(01)00095-1
Cupaioli FA, Zucca FA, Boraschi D, Zecca L (2014) Engineered nanoparticles. How brain friendly is this new guest? Prog Neurobiol 119–120:20–38. https://doi.org/10.1016/j.pneurobio.2014.05.002
Dash S, Murthy PN, Nath L, Chowdhury P (2010) Kinetic modeling on drug release from controlled drug delivery systems. Acta Pol Pharm 67:217–223. https://doi.org/10.1016/S0928-0987(01)00095-1
Desai N, Trieu V, Yao Z et al (2006) Increased antitumor activity, intratumor paclitaxel concentrations, and endothelial cell transport of cremophor-free, albumin-bound paclitaxel, ABI-007, compared with cremophor-based paclitaxel. Clin Cancer Res 12:1317–1324. https://doi.org/10.1158/1078-0432.CCR-05-1634
Desale JP, Swami R, Kushwah V et al (2018) Chemosensitizer and docetaxel-loaded albumin nanoparticle: overcoming drug resistance and improving therapeutic efficacy. Nanomedicine 13:2759-2776. https://doi.org/10.2217/nnm-2018-0206
Dreis S, Rothweiler F, Michaelis M et al (2007) Preparation, characterisation and maintenance of drug efficacy of doxorubicin-loaded human serum albumin (HSA) nanoparticles. Int J Pharm 341:207–214. https://doi.org/10.1016/j.ijpharm.2007.03.036
Drummond DC, Noble CO, Guo Z et al (2009) Improved pharmacokinetics and efficacy of a highly stable nanoliposomal vinorelbine. J Pharmacol Exp Ther 328:321–330. https://doi.org/10.1124/jpet.108.141200
Dube A, Nicolazzo JA, Larson I (2011) Assessment of plasma concentrations of (À) -epigallocatechin gallate in mice following administration of a dose reflecting consumption of a standard green tea beverage. Food Chem 128:7–13. https://doi.org/10.1016/j.foodchem.2011.02.038
Dudhipala N, Veerabrahma K (2015) Pharmacokinetic and pharmacodynamic studies of nisoldipine-loaded solid lipid nanoparticles developed by central composite design. Drug Dev Ind Pharm 41:1968–1977. https://doi.org/10.3109/03639045.2015.1024685
Elsadek B, Kratz F (2012) Impact of albumin on drug delivery—new applications on the horizon. J Control Release 157:4–28. https://doi.org/10.1016/j.jconrel.2011.09.069
Eng QY, Thanikachalam PV, Ramamurthy S (2018) Molecular understanding of Epigallocatechin gallate (EGCG) in cardiovascular and metabolic diseases. J Ethnopharmacol 210:296–310. https://doi.org/10.1016/j.jep.2017.08.035
Ferrado JB, Perez AA, Visentini FF et al (2018) Formation and characterization of self-assembled bovine serum albumin nanoparticles as chrysin delivery systems. Colloids Surf B Biointerfaces 173:43–51. https://doi.org/10.1016/j.colsurfb.2018.09.046
Freitas C, Müller RH (1998) Effect of light and temperature on zeta potential and physical stability in solid lipid nanoparticle (SLN®) dispersions. Int J Pharm 168:221–229. https://doi.org/10.1016/S0378-5173(98)00092-1
Fu Q, Sun J, Zhang W et al (2009) Nanoparticle albumin-bound (NAB) technology is a promising method for anti-cancer drug delivery. Recent Pat Anticancer Drug Discov 4:262–272. https://doi.org/10.2174/157489209789206869
Gallo JM, Hung CT, Perrier DG (1984) Analysis of albumin microsphere preparation. Int J Pharm 22:63–74. https://doi.org/10.1016/0378-5173(84)90046-2
Gradishar WJ, Tjulandin S, Davidson N et al (2005) Phase III trial of nanoparticle albumin-bound paclitaxel compared with polyethylated castor oil-based paclitaxel in women with breast cancer. J Clin Oncol 23:7794–7803. https://doi.org/10.1200/jco.2005.04.937
Hechler D, Nitsch R, Hendrix S (2006) Green-fluorescent-protein-expressing mice as models for the study of axonal growth and regeneration in vitro. Brain Res Rev 52:160–169. https://doi.org/10.1016/j.brainresrev.2006.01.005
Italia JL, Bhatt DK, Bhardwaj V et al (2007) PLGA nanoparticles for oral delivery of cyclosporine: nephrotoxicity and pharmacokinetic studies in comparison to Sandimmune Neoral®. J Control Release 119:197–206. https://doi.org/10.1016/j.jconrel.2007.02.004
Jithan A, Madhavi K, Madhavi M, Prabhakar K (2011) Preparation and characterization of albumin nanoparticles encapsulating curcumin intended for the treatment of breast cancer. Int J Pharm Investig 1:119. https://doi.org/10.4103/2230-973X.82432
Kalaria DR, Sharma G, Beniwal V, Ravi Kumar MNV (2009) Design of biodegradable nanoparticles for oral delivery of doxorubicin: in vivo pharmacokinetics and toxicity studies in rats. Pharm Res 26:492–501. https://doi.org/10.1007/s11095-008-9763-4
Karatas H, Aktas Y, Gursoy-ozdemir Y et al (2009) A nanomedicine transports a peptide caspase-3 inhibitor across the blood–brain barrier and provides neuroprotection. J Neurosci 29:13761–13769. https://doi.org/10.1523/jneurosci.4246-09.2009
Kim B, Lee C, Lee ES et al (2016) Paclitaxel and curcumin co-bound albumin nanoparticles having antitumor potential to pancreatic cancer. Asian J Pharm Sci 11:708–714. https://doi.org/10.1016/j.ajps.2016.05.005
Kratz F (2008) Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles. J Control Release 132:171–183. https://doi.org/10.1016/j.jconrel.2008.05.010
Krishna Sailaja A, Vineela C (2014) Preparation and characterization of mefenamic acid loaded bovine serum albumin nanoparticles by desolvation technique using acetone as desolvating agent. Der Pharm Lett 6:207–226. https://doi.org/10.2174/22117385046661605191
Kulandaivelu K, Mandal AKA (2017) Improved bioavailability and pharmacokinetics of tea polyphenols by encapsulation into gelatin nanoparticles. IET Nanobiotechnol 11:469–476. https://doi.org/10.1049/iet-nbt.2016.0147
Kumar G, Sharma S, Shafiq N et al (2011) Pharmacokinetics and tissue distribution studies of orally administered nanoparticles encapsulated ethionamide used as potential drug delivery system in management of multi-drug resistant tuberculosis. Drug Deliv 18:65–73. https://doi.org/10.3109/10717544.2010.509367
Kumar S, Meena R, Paulraj R (2016) Fabrication of BSA-green tea polyphenols-chitosan nanoparticles and their role in radioprotection: a molecular and biochemical approach. J Agric Food chem 64:6024–6034. https://doi.org/10.1021/acs.jafc.6b02068
Kumari M, Prasad M, Patnaik S, Shukla Y (2018) Curcumin loaded selenium nanoparticles synergize the anticancer potential of doxorubicin contained in self-assembled, cell receptor targeted nanoparticles. Eur J Pharm Biopharm 130:185–199. https://doi.org/10.1016/j.ejpb.2018.06.030
Lambert Joshua D, Yang Chung S (2003) Mechanisms of cancer prevention by tea constituents. J Nutr 133:3244S–3246S. https://doi.org/10.3945/ajcn.113.060186.Am
Lee JH, Shin YC, Yang WJ et al (2014) Epigallocatechin-3-O-gallate-loaded poly(lactic-co-glycolic acid) fibrous sheets as anti-adhesion barriers. J Biomed Nanotechnol 11:1461–1471. https://doi.org/10.1166/jbn.2015.2080
Leichsenring A, Bäcker I, Furtmüller PG et al (2016) Long-term effects of (−)-epigallocatechin gallate (EGCG) on pristane-induced arthritis (PIA) in female dark agouti rats. PLoS One 11:1–27. https://doi.org/10.1371/journal.pone.0152518
Li C, Zhang D, Guo Y et al (2014a) Galactosylated bovine serum albumin nanoparticles for parenteral delivery of oridonin: tissue distribution and pharmacokinetic studies. J Microencapsul 31:573–578. https://doi.org/10.3109/02652048.2014.898705
Li Z, Ha J, Zou T, Gu L (2014b) Fabrication of coated bovine serum albumin (BSA)-epigallocatechin gallate (EGCG) nanoparticles and their transport across monolayers of human intestinal epithelial Caco-2 cells. Food Funct 5:1278–1285. https://doi.org/10.1039/c3fo60500k
Lockman PR, Mumper RJ, Khan MA, Allen DD (2002) Nanoparticle technology for drug delivery across the blood–brain barrier. Drug Dev Ind Pharm 28:1–13. https://doi.org/10.1081/DDC-120001481
Merodioa M, Irachea JM, Eclancher F et al (2000) Distribution of albumin nanoparticles in animals induced with the experimental allergic encephalomyelitis. J Drug Target 8:289–303. https://doi.org/10.3109/10611860008997907
Nakagawa K, Okuda S, Miyazawa T (1997) Dose-dependent Incorporation of tea catechins, (−)-epigallocatechin-3-gallate and (−)-epigallocatechin, into human plasma. Biosci Biotechnol Biochem 61:1981–1985. https://doi.org/10.1271/bbb.61.1981
Nayak AP, Tiyaboonchai W, Patankar S et al (2010) Curcuminoids-loaded lipid nanoparticles: novel approach towards malaria treatment. Colloids Surf B Biointerfaces 81:263–273. https://doi.org/10.1016/j.colsurfb.2010.07.020
Pant MP, Mariam J, Joshi A, Dongre PM (2014) ScienceDirect UV radiation sensitivity of bovine serum albumin bound to silver nanoparticles. J Radiat Res Appl Sci 7:399–405. https://doi.org/10.1016/j.jrras.2014.07.004
Patel BK, Parikh RH, Aboti PS (2013) Development of oral sustained release rifampicin loaded chitosan nanoparticles by design of experiment. J Drug Deliv 2013:1–10. https://doi.org/10.1155/2013/370938
Pool H, Quintanar D, Figueroa JDD et al (2012) Antioxidant effects of quercetin and catechin encapsulated into PLGA nanoparticles. J Nanomater. 2012:1–12. https://doi.org/10.1155/2012/145380
Qi C, Chen Y, Jing QZ, Wang XG (2011) Preparation and characterization of catalase-loaded solid lipid nanoparticles protecting enzyme against proteolysis. Int J Mol Sci 12:4282–4293. https://doi.org/10.3390/ijms12074282
Radhakrishnan R, Kulhari H, Pooja D et al (2016) Encapsulation of biophenolic phytochemical EGCG within lipid nanoparticles enhances its stability and cytotoxicity against cancer. Chem Phys Lipids 198:51–60. https://doi.org/10.1016/j.chemphyslip.2016.05.006
Rahmani A, Al Shabrmi FM, Allemailem KS et al (2015) Implications of green tea and its constituents in the prevention of cancer via the modulation of cell signalling pathway. Biomed Res Int 2015:1–8. https://doi.org/10.1155/2015/925640
Ravi TP, Mandal AKA (2015) Effect of alcohol on release of green tea polyphenols from casein nanoparticles and its mathematical modeling. Res J Biotechnol 10:99–104
Rice-Evans CA, Miller NJ, Bolwell PG et al (1995) The relative antioxidant activities of plant-derived polyphenolic flavonoids. Free Radic Res 22:375–383
Saneja A, Nayak D, Srinivas M et al (2017) Development and mechanistic insight into enhanced cytotoxic potential of hyaluronic acid conjugated nanoparticles in CD44 overexpressing cancer cells. Elsevier B.V., Amsterdam
Sanoj Rejinold N, Muthunarayanan M, Chennazhi KP et al (2011) Curcumin loaded fibrinogen nanoparticles for cancer drug delivery. J Biomed Nanotechnol 7:521–534. https://doi.org/10.1166/jbn.2011.1320
Schroeder EK, Kelsey NA, Doyle J et al (2009) Green tea epigallocatechin 3-gallate accumulates in mitochondria and displays a selective antiapoptotic effect against inducers of mitochondrial oxidative stress in neurons. Antioxid Redox Signal 11:469–480. https://doi.org/10.1089/ars.2008.2215
Singh AK, Chakravarty B, Chaudhury K (2015) Nanoparticle-assisted combinatorial therapy for effective treatment of endometriosis. J Biomed Nanotechnol 11:789–804
Singh NA, Bhardwaj V, Ravi C et al (2018a) EGCG nanoparticles attenuate aluminum chloride induced neurobehavioral deficits, beta amyloid and tau pathology in a rat model of Alzheimer’s disease. Front Aging Neurosci 10:1–13. https://doi.org/10.3389/fnagi.2018.00244
Singh NA, Kalam A, Mandal A, Khan ZA (2018b) Inhibition of Al(III)-induced Aβ42 fibrillation and reduction of neurotoxicity by epigallocatechin-3-gallate nanoparticles. J Biomed Nanotechnol 14:1147–1158. https://doi.org/10.1166/jbn.2018.2552
Stringer M, Abeysekera I, Thomas J et al (2017) Epigallocatechin-3-gallate (EGCG) consumption in the Ts65Dn model of Down syndrome fails to improve behavioral deficits and is detrimental to skeletal phenotypes. Physiol Behav. https://doi.org/10.1016/j.physbeh.2017.05.003
Suresh G, Manjunath K, Venkateswarlu V, Satyanarayana V (2007) Preparation, characterization, and in vitro and in vivo evaluation of lovastatin solid lipid nanoparticles. AAPS PharmSciTech 8:24. https://doi.org/10.1208/pt0801024
Syame SM, Eisa ZM, Eltayeb R et al (2018) Synthesis and characterization of cisplatin-loaded BSA (bovine serum albumin) nanoparticles as drug delivery system against pancreatic cancer cells. IOSR J Pharm 8:39–48
Tang QS, Chen DZ, Xue WQ et al (2011) Preparation and biodistribution of 188Re-labeled folate conjugated human serum albumin magnetic cisplatin nanoparticles (188Re-folate-CDDP/HSA MNPs) in vivo. Int J Nanomed 6:3077–3085. https://doi.org/10.2147/IJN.S24322
Thangapazham RL, Singh AK, Sharma A et al (2007) Green tea polyphenols and its constituent epigallocatechin gallate inhibits proliferation of human breast cancer cells in vitro and in vivo. Cancer Lett 245:232–241. https://doi.org/10.1016/j.canlet.2006.01.027
Tian X, Yang X, Wang K, Yang X (2006) The efflux of flavonoids morin, isorhamnetin-3-O-rutinoside and diosmetin-7-O-β-d-xylopyranosyl-(1-6)-β-d-glucopyranoside in the human intestinal cell line Caco-2. Pharm Res 23:1721–1728. https://doi.org/10.1007/s11095-006-9030-5
Tominari T, Matsumoto C, Watanabe K et al (2015) Epigallocatechin gallate (EGCG) suppresses lipopolysaccharide-induced inflammatory bone resorption, and protects against alveolar bone loss in mice. FEBS Open Bio 5:522–527. https://doi.org/10.1016/j.fob.2015.06.003
Ulbrich K, Michaelis M, Rothweiler F et al (2011) Interaction of folate-conjugated human serum albumin (HSA) nanoparticles with tumour cells. Int J Pharm 406:128–134. https://doi.org/10.1016/j.ijpharm.2010.12.023
Vivek K, Reddy H, Murthy RSR (2007) Investigations of the effect of the lipid matrix on drug entrapment, in vitro release, and physical stability of olanzapine-loaded solid lipid nanoparticles. AAPS PharmSciTech 8:E83. https://doi.org/10.1208/pt0804083
Weber C, Coester C, Kreuter J, Langer K (2000) Desolvation process and surface characterisation of protein nanoparticles. Int J Pharm 194:91–102. https://doi.org/10.1016/S0378-5173(99)00370-1
Weinreb O, Mandel S, Amit T, Youdim MB (2004) Neurological mechanisms of green tea polyphenols in Alzheimer’ s and Parkinson’ s diseases. J Nutr Biochem 15:506–516. https://doi.org/10.1016/j.jnutbio.2004.05.002
Woods A, Patel A, Spina D et al (2015) In vivo biocompatibility, clearance, and biodistribution of albumin vehicles for pulmonary drug delivery. J Control Release 210:1–9. https://doi.org/10.1016/j.jconrel.2015.05.269
Yang CS, Chen L, Lee M-J, Balentine D, Kuo MC, Schantz SP (1998) Blood and urine levels of tea catechins after ingestion of different amounts of green tea by human volunteers. Cancer Epidemiol Biomarkers Prev 7:351–354
Yang L, Cui F, Cun D et al (2007) Preparation, characterization and biodistribution of the lactone form of 10-hydroxycamptothecin (HCPT)-loaded bovine serum albumin (BSA) nanoparticles. Int J Pharm 340:163–172. https://doi.org/10.1016/j.ijpharm.2007.03.028
Yedomon B, Fessi H, Charcosset C (2013) Preparation of bovine serum albumin (BSA) nanoparticles by desolvation using a membrane contactor: a new tool for large scale production. Eur J Pharm Biopharm 85:398–405. https://doi.org/10.1016/j.ejpb.2013.06.014
Yu Z, Yu M, Zhang Z et al (2014) Bovine serum albumin nanoparticles as controlled release carrier for local drug delivery to the inner ear. 9:1–7. https://doi.org/10.1186/1556-276X-9-343
Zhang L, Zheng Y, Chow MSS, Zuo Z (2004) Investigation of intestinal absorption and disposition of green tea catechins by Caco-2 monolayer model. Int J Pharm 287:1–12. https://doi.org/10.1016/j.ijpharm.2004.08.020
Zhang H, Huang N, Yang G et al (2017) Bufalin-loaded bovine serum albumin nanoparticles demonstrated improved anti-tumor activity against hepatocellular carcinoma: preparation, characterization, pharmacokinetics and tissue distribution. Oncotarget 8:63311–63323. https://doi.org/10.18632/oncotarget.18800
Zhao D, Zhao X, Zu Y et al (2010) Preparation, characterization, and in vitro targeted delivery of folate-decorated paclitaxel-loaded bovine serum albumin nanoparticles. Int J Nanomed 5:669–677. https://doi.org/10.2147/IJN.S12918
Acknowledgements
The authors are thankful to NTRF, Tea Board, Kolkata for providing financial support. The authors are also thankful to the management of VIT for providing necessary facilities. We would also thank Sun Pharmaceutical Industrial limited, India for sample analysis.
Funding
Funding was provided by National Tea Research Foundation, Tea Board, Kolkata (17(330)/214).
Author information
Authors and Affiliations
Contributions
AKAM was responsible for the concept and design of this study. NR performed all the experiments and compiled the results. NR and AKAM analyzed the data and drafted the manuscript. AKAM performed the final critical revision of the manuscript. All authors have read and approved the final manuscript.
Corresponding author
Ethics declarations
Conflict of interest
The authors declare no conflict of interest.
Rights and permissions
About this article
Cite this article
Ramesh, N., Mandal, A.K.A. Encapsulation of epigallocatechin-3-gallate into albumin nanoparticles improves pharmacokinetic and bioavailability in rat model. 3 Biotech 9, 238 (2019). https://doi.org/10.1007/s13205-019-1772-y
Received:
Accepted:
Published:
DOI: https://doi.org/10.1007/s13205-019-1772-y