Vardenafil Improves the Proliferative Inhibition of EGCG-β-lactoglobulin Nanoparticles Against Liver Cancer Cells

CHEN Chunxiao, LOU Wenyu, DING Zhenjian, LI Zhuoye, YANG Yuanyuan, JIN Peng, DU Qizhen

Journal of Tea Science ›› 2020, Vol. 40 ›› Issue (4) : 528-535.

PDF(1695 KB)
PDF(1695 KB)
Journal of Tea Science ›› 2020, Vol. 40 ›› Issue (4) : 528-535. DOI: 10.13305/j.cnki.jts.2020.04.009
Research Paper

Vardenafil Improves the Proliferative Inhibition of EGCG-β-lactoglobulin Nanoparticles Against Liver Cancer Cells

  • CHEN Chunxiao, LOU Wenyu, DING Zhenjian, LI Zhuoye, YANG Yuanyuan, JIN Peng, DU Qizhen*
Author information +
History +

Abstract

The combination of nano and other drugs is an important strategy to improve the biological activity of EGCG, since a high EGCG concentration is essential for the inhibition of the proliferation of cancer cells. In this study, EGCG-vardenafil (VD)-β-lactoglobulin (β-Lg)-nanoparticles (EVβ-NPs) was prepared by encapsulating EGCG and VD in β-Lg nano-carriers. In vitro experimental results show that EVβ-NPs could upgrade the activity of caspase-3 in HepG2 cells compared to the native EGCG, which caused cell cycle arrest in the S phase of HepG2 cells to induce cell nuclear division, and finally lead to HepG2 cell apoptosis. The results demonstrate that the encapsulation of EGCG-VD can significantly improve the anticancer activity of EGCG, and possesses potential value in the development of EGCG anticancer products.

Key words

β-lactoglobulin / EGCG / nanoparticles / proliferative inhibition / vardenafil

Cite this article

Download Citations
CHEN Chunxiao, LOU Wenyu, DING Zhenjian, LI Zhuoye, YANG Yuanyuan, JIN Peng, DU Qizhen. Vardenafil Improves the Proliferative Inhibition of EGCG-β-lactoglobulin Nanoparticles Against Liver Cancer Cells[J]. Journal of Tea Science. 2020, 40(4): 528-535 https://doi.org/10.13305/j.cnki.jts.2020.04.009

References

[1] 刘超, 陈若芸. 儿茶素及其类似物的化学和生物活性研究进展[J]. 中国中药杂志, 2004, 29(10): 1017-1021.
Liu C, Chen R Y.Advance of chemistry and bioactivities of catechin and its analogues[J]. China Journal of Chinese Materia Medica, 2004, 29(10): 1017-1021.
[2] Ponniah K, Loo T S, Edwards P J, et al.The production of soluble and correctly folded recombinant bovine β-lactoglobulin variants A and B in Escherichia coli for NMR studies[J]. Protein Expr Purifi, 2010, 70(2): 283-289.
[3] Liang L, Tajmir-Riahi H A, Subirade M. Interaction of β-lactoglobulin with resveratrol and its biological implications[J]. Biomacromolecules, 2008, 9: 50-56.
[4] Sneharani A H, Karakkat J V, Singly S A.Interaction of curcumin with β-lactoglobulin stability, spectroscopic analysis, and molecular modeling of the complex[J]. Journal of Agricultural and Food Chemistry, 2010, 58: 11130-11139.
[5] Zimet P, Livney Y D.Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for ω-3 polyunsaturated fatty acids[J]. Food Hydrocoll, 2009, 23: 1120-1126.
[6] Kumazoe M, Sugihara K, Tsukamoto S, et al.67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis[J]. J Clin Invest, 2013, 123(2): 787-99.
[7] 黄美蓉, 应浩, 江用文, 等. EGCG纳米粒的制备及其抗肿瘤活性研究[J]. 茶叶科学, 2015, 35(6): 605-612.
Huang M R, Ying H, Jiang Y W, et al.Research on preparation and antitumor activity of EGCG naonparticles[J]. Journal of Tea Science, 2015, 35(6): 605-612.
[8] Shpigelman A, Israeli G, Livney Y D.Thermally-induced protein-polyphenol co-assemblies: beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG[J]. Food Hydrocoll, 2010, 24(8): 735-743.
[9] Li B, Du W, Jin J, et al.Preservation of (-)-epigallocatechin-3-gallate antioxidant properties loaded in heat treated β-lactoglobulin nanoparticles[J]. J Agriculture Food Chemistry, 2012, 60: 3477-3484.
[10] 成惠林. 检测细胞活性的MTT方法[J]. 江苏医药, 1996, 22(5): 330-331.
Cheng H L.MTT method for the detection of cell activity[J]. Jinagsu Med J, 1996, 22(5): 330-331.
[11] 周建军, 乐秀芳, 韩家娴, 等. 影响MTT方法测定结果的一些因素[J]. 肿瘤, 1994, 14(2): 93-94.
Zhou J J, Le X F, Han J X, et al.The factors influencing the results of MTT[J]. Tumor, 1994, 14(2): 93-94.
[12] Mu?ller R H, Jacobs C, Kayser O. Nanosuspensions as particulate drug formulations in therapy rationale for development and what we can expect for the future[J]. Adv Drug Delivery Rev, 2001(47): 3-19.
[13] Timasheff S N, Townend R.Molecular interactions in β-lactoglobulin. I. The association of the genetic species of β-lactoglobulin below the isoelectric point[J]. J Am Chem Soc, 1961, 83(2): 464-469.
[14] Chithrani B D, Ghazani A A, Chan W C W. Determining the size and shape dependence of gold nanoparticle uptake into mammalian cells[J]. Nano Lett, 2006, 6: 662-668.
[15] Yang C S, Wang X, Lu G, et al.Cancer prevention by tea: animal studies, molecular mechanisms and human relevance[J]. Nat Rev Cancer 2009, 9: 429-439.
[16] Wu M, Jin J, Jin P, et al.Epigallocatechin gallate-β-lactoglobulin nanoparticles improve the antitumor activity of EGCG for inducing cancer cell apoptosis[J]. J Funct Food, 2017, 39: 257-263.
[17] Fan Y, Zhang Y, Yokoyama W, et al.β-Lactoglobulin-chlorogenic acid conjugate-based nanoparticles for delivery of (-)-epigallocatechin-3-gallate[J]. RSC Adv, 2017, 7(35): 21366-21374.
[18] Yang Y, Jin P, Zhang X, et al.New epigallocatechin gallate (EGCG) nanocomplexes co-assembled with 3-mercapto-1-Hexanol and β-lactoglobulin for improvement of antitumor activity[J]. J Biomedi Nanotechnol, 2017, 13(7): 805-814.
[19] Zhang L, Sahu I D, Xu M, et al.Effect of metal ions on the binding reaction of (-)-epigallocatechin gallate to β-lactoglobulin[J]. Food Chemistry, 2017, 221: 1923-1929.
[20] Corbin J D, Beasley A, Blount M A, et al.Vardenafil: structural basis for higher potency over sildenafil in inhibiting cGMP specific phosphodiesterase-5 (PDE5)[J]. Neurochem Int, 2004, 45: 859-863.
[21] Li Q, Shu Y.Pharmacological modulation of cytotoxicity and cellular uptake of anti-cancer drugs by PDE5 Inhibitors in lung cancer cells[J]. Pharma Res, 2014, 31: 86-96.
PDF(1695 KB)

Accesses

Citation

Detail

Sections
Recommended

/