In situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies

Priyanka Singh,1,2 Yeon Ju Kim,1 Hina Singh,1 Sungeun Ahn,1 Verónica Castro-Aceituno,1 Deok Chun Yang1,2 1Department of Oriental Medicine Biotechnology, Ginseng Bank, 2Graduate School of Biotechnology, College of Life Sciences, Kyung Hee University, Yongin, Republic of Korea Abstract: T...

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Autores principales:	Singh P, Kim YJ, Singh H, Ahn S, Castro-Aceituno V, Yang DC
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2017
Materias:	Bovine serum albumin Ginsenoside Rh2 Solubility Stability Cancer Inflammation. Medicine (General) R5-920
Acceso en línea:	https://doaj.org/article/534338adb0aa41dca32761455594307c
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spelling	oai:doaj.org-article:534338adb0aa41dca32761455594307c2021-12-02T01:32:30ZIn situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies1178-2013https://doaj.org/article/534338adb0aa41dca32761455594307c2017-05-01T00:00:00Zhttps://www.dovepress.com/in-situ-preparation-of-water-soluble-ginsenoside-rh2-entrapped-bovine--peer-reviewed-article-IJNhttps://doaj.org/toc/1178-2013Priyanka Singh,1,2 Yeon Ju Kim,1 Hina Singh,1 Sungeun Ahn,1 Verónica Castro-Aceituno,1 Deok Chun Yang1,2 1Department of Oriental Medicine Biotechnology, Ginseng Bank, 2Graduate School of Biotechnology, College of Life Sciences, Kyung Hee University, Yongin, Republic of Korea Abstract: The present study investigates a simple and convenient one-step procedure for the preparation of bovine serum albumin (BSA)-Rh2 nanoparticles (NPs) at room temperature. In this work, ginsenoside Rh2 was entrapped within the BSA protein to form BSA-Rh2 NPs to enhance the aqueous solubility, stability, and therapeutic efficacy of Rh2. The physiochemical characterization by high-performance liquid chromatography, nuclear magnetic resonance, Fourier transform infrared spectroscopy, field emission transmission electron microscopy, dynamic light scattering, and thermogravimetric analysis confirmed that the prepared BSA-Rh2 NPs were spherical, highly monodispersed, and stable in aqueous systems. In addition, the stability of NPs in terms of different time intervals, pHs, and temperatures (20°C–700°C) was analyzed. The results obtained with different pHs showed that the synthesized BSA-Rh2 NPs were stable in the physiological buffer (pH 7.4) for up to 8 days, but degraded under acidic conditions (pH 5.0) representing the pH inside tumor cells. Furthermore, comparative analysis of the water solubility of BSA-Rh2 NPs and standard Rh2 showed that the BSA nanocarrier enhanced the water solubility of Rh2. Moreover, in vitro cytotoxicity assays including cell viability assays and morphological analyses revealed that Rh2-entrapped BSA NPs, unlike the free Rh2, demonstrated better in vitro cell viability in HaCaT skin cell lines and that BSA enhanced the anticancer effect of Rh2 in A549 lung cell and HT29 colon cancer cell lines. Additionally, anti-inflammatory assay of BSA-Rh2 NPs and standard Rh2 performed using RAW264.7 cells revealed decreased lipopolysaccharide-induced nitric oxide production by BSA-Rh2 NPs. Collectively, the present study suggests that BSA can significantly enhance the therapeutic behavior of Rh2 by improving its solubility and stability in aqueous systems, and hence, BSA-Rh2 NPs may potentially be used as a ginsenoside delivery vehicle in cancer and inflammatory cell lines. Keywords: bovine serum albumin, ginsenoside Rh2, solubility, stability, cancer, inflammationSingh PKim YJSingh HAhn SCastro-Aceituno VYang DCDove Medical PressarticleBovine serum albuminGinsenoside Rh2SolubilityStabilityCancerInflammation.Medicine (General)R5-920ENInternational Journal of Nanomedicine, Vol Volume 12, Pp 4073-4084 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Bovine serum albumin Ginsenoside Rh2 Solubility Stability Cancer Inflammation. Medicine (General) R5-920
spellingShingle	Bovine serum albumin Ginsenoside Rh2 Solubility Stability Cancer Inflammation. Medicine (General) R5-920 Singh P Kim YJ Singh H Ahn S Castro-Aceituno V Yang DC In situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies
description	Priyanka Singh,1,2 Yeon Ju Kim,1 Hina Singh,1 Sungeun Ahn,1 Verónica Castro-Aceituno,1 Deok Chun Yang1,2 1Department of Oriental Medicine Biotechnology, Ginseng Bank, 2Graduate School of Biotechnology, College of Life Sciences, Kyung Hee University, Yongin, Republic of Korea Abstract: The present study investigates a simple and convenient one-step procedure for the preparation of bovine serum albumin (BSA)-Rh2 nanoparticles (NPs) at room temperature. In this work, ginsenoside Rh2 was entrapped within the BSA protein to form BSA-Rh2 NPs to enhance the aqueous solubility, stability, and therapeutic efficacy of Rh2. The physiochemical characterization by high-performance liquid chromatography, nuclear magnetic resonance, Fourier transform infrared spectroscopy, field emission transmission electron microscopy, dynamic light scattering, and thermogravimetric analysis confirmed that the prepared BSA-Rh2 NPs were spherical, highly monodispersed, and stable in aqueous systems. In addition, the stability of NPs in terms of different time intervals, pHs, and temperatures (20°C–700°C) was analyzed. The results obtained with different pHs showed that the synthesized BSA-Rh2 NPs were stable in the physiological buffer (pH 7.4) for up to 8 days, but degraded under acidic conditions (pH 5.0) representing the pH inside tumor cells. Furthermore, comparative analysis of the water solubility of BSA-Rh2 NPs and standard Rh2 showed that the BSA nanocarrier enhanced the water solubility of Rh2. Moreover, in vitro cytotoxicity assays including cell viability assays and morphological analyses revealed that Rh2-entrapped BSA NPs, unlike the free Rh2, demonstrated better in vitro cell viability in HaCaT skin cell lines and that BSA enhanced the anticancer effect of Rh2 in A549 lung cell and HT29 colon cancer cell lines. Additionally, anti-inflammatory assay of BSA-Rh2 NPs and standard Rh2 performed using RAW264.7 cells revealed decreased lipopolysaccharide-induced nitric oxide production by BSA-Rh2 NPs. Collectively, the present study suggests that BSA can significantly enhance the therapeutic behavior of Rh2 by improving its solubility and stability in aqueous systems, and hence, BSA-Rh2 NPs may potentially be used as a ginsenoside delivery vehicle in cancer and inflammatory cell lines. Keywords: bovine serum albumin, ginsenoside Rh2, solubility, stability, cancer, inflammation
format	article
author	Singh P Kim YJ Singh H Ahn S Castro-Aceituno V Yang DC
author_facet	Singh P Kim YJ Singh H Ahn S Castro-Aceituno V Yang DC
author_sort	Singh P
title	In situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies
title_short	In situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies
title_full	In situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies
title_fullStr	In situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies
title_full_unstemmed	In situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies
title_sort	in situ preparation of water-soluble ginsenoside rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies
publisher	Dove Medical Press
publishDate	2017
url	https://doaj.org/article/534338adb0aa41dca32761455594307c
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In situ preparation of water-soluble ginsenoside Rh2-entrapped bovine serum albumin nanoparticles: in vitro cytocompatibility studies

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