scholarly journals Design and development of paclitaxel-loaded bovine serum albumin nanoparticles for brain targeting

2011 ◽  
Vol 61 (2) ◽  
pp. 141-156 ◽  
Author(s):  
Amit Bansal ◽  
Deepak Kapoor ◽  
Rishi Kapil ◽  
Neha Chhabra ◽  
Sanju Dhawan
Keyword(s):  
Electron Microscopy ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Correlation Spectroscopy ◽  
Brain Targeting ◽  
Release Mechanism ◽  
Design And Development ◽  
Albumin Nanoparticles

Design and development of paclitaxel-loaded bovine serum albumin nanoparticles for brain targeting Bovine serum albumin (BSA) nanoparticles loaded with paclitaxel (PTX) were prepared using a desolvation technique. A 32 full factorial design (FFD) was employed to formulate nanoparticles. Nanoparticles were characterized for particle size by photon correlation spectroscopy and surface morphology by scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Encapsulation efficiency, zeta potential and particle yield were also determined. Response surface linear modelling (RSLM) was used to predict the optimal formulation. Various models were applied to determine the release mechanism from PTX nanoparticles. The effect of drug-polymer ratio on the release profile of formulations was observed and was applied to determine the suitability of the predicted optimal formulation. A preliminary study to determine the feasibility of targeting the prepared nanoparticles to brain was also carried out using mice as in vivo models.

UCNP@BSA@Ru nanoparticles with tumor-specific and NIR-triggered efficient PACT activity in vivo

2021 ◽  
Author(s):  
Chao Zhang ◽  
Xusheng Guo ◽  
Xuwen Da ◽  
Yishan Yao ◽  
Haihua Xiao ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Short Wavelength ◽  
Ru Nanoparticles ◽  
Wavelength Absorption ◽  
Tumor Accumulation ◽  
Accumulation Ability

Ru(II)-based photoactivated chemotherapy (PACT) agents are promising, however, the short wavelength absorption (generally < 550 nm) and poor tumor accumulation ability limit their in vivo applications. Herein bovine serum albumin...

Transfecting pDNA to E . coli DH5α using bovine serum albumin nanoparticles as a delivery vehicle

Luminescence ◽  
2014 ◽  
Vol 30 (5) ◽  
pp. 583-591 ◽  
Author(s):  
Jitendra Wagh ◽  
Kuldeep J. Patel ◽  
Parth Soni ◽  
Krutika Desai ◽  
Pratik Upadhyay ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Delivery Vehicle ◽  
E Coli ◽  
Albumin Nanoparticles

BSA directed-synthesis of biocompatible Fe3O4 nanoparticles for dual-modal T1 and T2 MR imaging in vivo

2017 ◽  
Vol 9 (21) ◽  
pp. 3099-3104 ◽  
Author(s):  
Dong Li ◽  
Minghui Hua ◽  
Kun Fang ◽  
Rong Liang
Keyword(s):  
Bovine Serum Albumin ◽  
Mr Imaging ◽  
Serum Albumin ◽  
Fe3o4 Nanoparticles ◽  
Bovine Serum ◽  
Mild Conditions ◽  
Directed Synthesis ◽  
T1 And T2

Bovine serum albumin-Fe3O4 nanoparticles with undoubted biosafety and robust dual-modal T1 and T2 MR imaging ability were fabricated using a biomineralization approach in a facile way under mild conditions for in vivo MR imaging.

scholarly journals Clearance and binding of native and defucosylated lactoferrin

1983 ◽  
Vol 212 (2) ◽  
pp. 249-257 ◽  
Author(s):  
M J Imber ◽  
S V Pizzo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Binding ◽  
Gel Filtration ◽  
Peritoneal Macrophages ◽  
Mononuclear Phagocyte ◽  
Stable Complex

These studies explore the role of carbohydrate recognition systems and the direct involvement of terminal alpha 1-3-linked fucose in the clearance of lactoferrin from the murine circulation and in the specific binding of lactoferrin to receptors on murine peritoneal macrophages. As previously reported, radiolabelled lactoferrin cleared very rapidly (t1/2 less than 1 min) after intravenous injection into mice. However, competing levels of ligands specific for the hepatic galactose receptor (asialo-orosomucoid), the hepatic fucose receptor (fucosyl-bovine serum albumin), and the mononuclear-phagocyte system pathway recognizing mannose, N-acetylglucosamine and fucose (mannosyl-, N-acetylglucosaminyl- and fucosyl-bovine serum albumin) did not block radiolabelled lactoferrin clearance in vivo or binding to mouse peritoneal macrophage monolayers in vitro. Almond emulsin alpha 1-3-fucosidase was used to prepare defucosylated lactoferrin in which 88% of the alpha 1-3-linked fucose was hydrolysed. No difference in clearance or receptor binding was observed between radiolabelled native and defucosylated lactoferrin. Fucoidin, a fucose-rich algal polysaccharide, completely inhibits the clearance in vivo and macrophage binding in vitro of lactoferrin. This effect, however, is probably not the result of competition for binding to the fucose receptor, since gel-filtration studies demonstrated formation of a stable complex between lactoferrin and fucoidin. The present results indicate that the lactoferrin-clearance pathway is distinct from several pathways mediating glycoprotein clearance through recognition of terminal galactose, fucose, N-acetylglucosamine or mannose. Furthermore, alpha 1-3-linked fucose on lactoferrin is not essential for lactoferrin clearance in vivo or specific binding to macrophage receptors in vitro.

Corona protein impacts on alternating current biosusceptometry signal and circulation times of differently coated MnFe2O4 nanoparticles

Nanomedicine ◽  
2021 ◽  
Author(s):  
Andre Gonçalves Prospero ◽  
Lais Pereira Buranello ◽  
Carlos AH Fernandes ◽  
Lucilene Delazari dos Santos ◽  
Guilherme Soares ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Signal Intensity ◽  
Alternating Current ◽  
Circulation Time ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

Background: We evaluated the impacts of corona protein (CP) formation on the alternating current biosusceptometry (ACB) signal intensity and in vivo circulation times of three differently coated magnetic nanoparticles (MNP): bare, citrate-coated and bovine serum albumin-coated MNPs. Methods: We employed the ACB system, gel electrophoresis and mass spectrometry analysis. Results: Higher CP formation led to a greater reduction in the in vitro ACB signal intensity and circulation time. We found fewer proteins forming the CP for the bovine serum albumin-coated MNPs, which presented the highest circulation time in vivo among the MNPs studied. Conclusion: These data showed better biocompatibility, stability and magnetic signal uniformity in biological media for bovine serum albumin-coated MNPs than for citrate-coated MNPs and bare MNPs.

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