scholarly journals Bovine Serum Albumin-Loaded Chitosan/Dextran Nanoparticles: Preparation and Evaluation ofEx VivoColloidal Stability in Serum

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Haliza Katas ◽  
Zahid Hussain ◽  
Siti Asarida Awang
Keyword(s):  
Particle Size ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Colloidal Stability ◽  
Ex Vivo ◽  
Biological Fluids ◽  
Chitosan Nanoparticles ◽  
Physiological Model

Chitosan (CS) nanoparticles have several distinct intrinsic advantages; however, theirin vivocolloidal stability in biological fluids was not fully explored especially when carrying proteins. The present study aimed to investigate their colloidal stability using anex vivophysiological model of fetal bovine serum (FBS) and human serum (HS). The stability of bovine-serum-albumin (BSA-) loaded nanoparticles was relatively higher in FBS than that in HS. Particle size of unloaded and BSA-loaded nanoparticles was statistically unchanged up to 24 h after incubation in FBS. However in HS, a significant increase in particle size from 144 ± 17 to 711 ± 22 nm was observed for unloaded nanoparticles and by 2.5-fold for BSA-loaded nanoparticle, at 24 h after incubation in HS. Zeta potential of both nanoparticles was less affected by the components in FBS compared to those in HS. A remarkable swelling extent was experienced for unloaded and BSA-loaded nanoparticles in HS, up to 54 ± 4% and 44 ± 5%, respectively. Morphology of unloaded and BSA-loaded nanoparticles was varied from smooth spherical and rod shape to irregular shape when incubated in FBS; however, form agglomerates when incubated in HS. These findings therefore suggest that HS is more reactive to cause colloidal instability to the chitosan nanoparticles compared to FBS.

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...

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.

Box-Behnken Design Optimized TPGS Coated Bovine Serum Albumin Nanoparticles Loaded with Anastrozole

2021 ◽  
Vol 18 ◽  
Author(s):  
Ashish Kumar ◽  
Ajit Singh ◽  
S.J.S Flora ◽  
Rahul Shukla
Keyword(s):  
Particle Size ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Glycol Succinate ◽  
Burst Release ◽  
Spectroscopic Techniques ◽  
Potential Candidate ◽  
Box Behnken Design ◽  
Thermal Gelation

Purpose: In this study, a novel D-α-tocopheryl polyethylene glycol succinate (TPGS) modified bovine serum albumin (BSA) nanoparticles were developed for delivery of Anastrozole (ANZ) which is optimized by Box-Behnken design (BBD). This TPGS-ANZ-BSA NPs are evaluated for their physicochemical and drug release characteristics. Methods: TPGS-ANZ-BSA NPs were prepared by desolvation thermal gelation method andthe effects of critical process parameter (CPP)which are BSA amount, TPGS concentration and stirring speed on the critical quality attributes (CQA) such as % drug loading (%DL) and particle size were studied using BBD. TPGS-ANZ-BSA NPs were characterized using different spectroscopic techniques including UV-Visible and FTIR is used to confirm the entrapment of ANZ in BSA. DSC and PXRD revealed the amorphization of ANZ in the TPGS-ANZ-BSA NPs after freeze drying. Scanning electron microscopy (SEM) analysis was performed for the surface morphologyanalysesNPs. In vitro release studies were performed at pH 5.5 and pH 7.4 for 48h to mimic tumour microenvironment. Results: The BBD optimized batch showed 107 nm particle size with % DL of 8.5± 0.5 of TPGS-ANZ-BSA NPs. The spectroscopic and thermal characterizations revealed the successful encapsulation of ANZ inside the nanoparticles.The TPGS-ANZ-BSA NPs were found to exhibit burst release at pH 5.5 and sustained release at pH 7.4. The short-term stability of drug-loaded nanoparticles displayed no significant changes in physicochemical properties at room temperature for period of one month. Conclusion: The BBD optimized TPGS-ANZ-BSA nanoparticles showed enhanced physiochemical properties for ANZ and potential candidate for anticancer agent drugs delivery.

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.

Chemotactic properties, cellular binding and uptake of peptides and peptide derivatives: studies with Tetrahymena thermophila

1992 ◽  
Vol 103 (2) ◽  
pp. 565-570
Author(s):  
V. Leick
Keyword(s):  
Bovine Serum Albumin ◽  
Cell Surface ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Tetrahymena Thermophila ◽  
Chemotactic Peptide ◽  
Dansyl Group ◽  
Peptide Derivatives

Receptor-mediated binding of leukocyte chemotactic peptide, N-formylMet-Leu-Phe (fMLP), occurs in the ciliated protozoon Tetrahymena thermophila. In vivo labelling of the cells with N-formylMet-Leu-[3H]Phe ([3H]fMLP) shows that the cells bind the ligand with high affinity (KD = 4 × 10(−9) M to 1 × 10(−8) M). Moreover, Scatchard transformations of the binding data show that there are about 5 × 10(5) binding sites per cell on the cell surface. Two fluorescent derivatives of leukocyte chemotactic peptide, N-dansylMet-Leu-Phe (dansMLP) and N-formylMet-Leu-Phe-(N-dansyl-)Lys (fMLPdanLys) compete for the N-formylMet-Leu-Phe (fMLP) binding sites on the cell surface. Moreover, both derivatives have retained significant chemoattracting potentials. Fluorescence from dansMLP, but not from fMLPdansLys and dansyl-beta-endorphin, is internalized preferentially into small vesicles. The differences may, however, reflect that the fluorescence from the dansyl group is strongly quenched by a hydrophilic microenvironment when using the two latter peptide derivatives. In contrast, the dansyl group from dansMLP must be assumed to be embedded in a hydrophobic microenvironment in the vesicular membrane or membrane protein. Rhodamine-labelled bovine serum albumin, egg albumin and cytochrome c as well as dansylated bovine serum albumin, which are poor chemoattractants, are preferentially seen to be internalized into large vesicles (food vacuoles).

Quality by Design Approach for Development and Optimization of Rifampicin Loaded Bovine Serum Albumin Nanoparticles and Characterization

2021 ◽  
Vol 18 ◽  
Author(s):  
Monica Joshi ◽  
Khushwant S. Yadav ◽  
Bala Prabhakar
Keyword(s):  
Particle Size ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Quality By Design ◽  
Entrapment Efficiency ◽  
Quality Attributes ◽  
Albumin Nanoparticles ◽  
Therapeutic Benefits ◽  
Intravenous Application

Background: Rifampicin is one of the first line drugs used for tuberculosis therapy. The therapy lasts for a long time. Thus, there is a need to develop sustained release formulation of rifampicin for intravenous application. Aim: This study is focused on preparing rifampicin loaded bovine serum albumin nanoparticles (RIF BSA NPs) suitable for intravenous application using systematic quality by design (QbD) approach. Objectives: The main objective of this study is optimizing particle size and entrapment efficiency of rifampicin loaded bovine serum albumin nanoparticles (RIF BSA NPs) and making it suitable for intravenous application using QbD approach. Methods: Quality target product profile was defined along with critical quality attributes (CQAs) for the formulation. 32 factorial design was used for achieving the predetermined values of CQAs, i.e., mean particle size <200 nm and percent entrapment efficiency>50%. Incubation time of drug with colloidal albumin solution and ratio of rifampicin: albumin, were selected as independent variables. Check point analysis was performed to confirm the suitability of regression model for optimization. Results: : The optimized RIF BSA NPs were characterized by FTIR, DSC, 1H NMR techniques. The NPs observed by transmission electron microscopy were spherical in shape. The rifampicin release could be sustained for 72 hours from BSA NPs matrix. RIF BSA NPs dispersion was stable at 5 ± 3°C for 72 hours. Non-toxicity of nanoparticles to RAW 264.7 cell line was proved by MTT assay. Conclusion: Development of RIF BSA NPs with desired quality attributes was possible by implementing QbD approach. The optimized formulation suitable for intravenous application can potentially improve the therapeutic benefits of rifampicin.

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