scholarly journals Preparation and Characterization of Irinotecan Loaded Cross-Linked Bovine Serum Albumin Beads for Liver Cancer Chemoembolization Therapy

2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
Jin Yan ◽  
Fei Wang ◽  
Jun Chen ◽  
Tao Liu ◽  
Tao Zhang
Keyword(s):  
Bovine Serum Albumin ◽  
Liver Cancer ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Rabbit Model ◽  
Drug Carriers ◽  
Embolic Agent ◽  
Diffusion Method ◽  
Liver Carcinoma ◽  
Burst Release

In this paper, a novel temporary embolization agent for transarterial chemoembolization of liver cancer was developed and tested. The Irinotecan loaded bovine serum albumin (BSA) beads were tried to be used as embolic agent of liver cancer therapy. BSA beads were prepared by a water-in-oil emulsion solvent diffusion method in soya oil and Span 85 was used as the emulsifier. The obtained BSA beads were able to swell 2.37-fold comparing to dried beads. Depending on the equilibrium swelling process, the Irinotecan was loaded with 9.8% total drug concentration and tested. In vitro drug release studies showed that a burst release of Irinotecan was achieved. Eventually BSA beads were completely degraded in a few weeks. CCK-8 assay demonstrated that BSA beads showed no cytotoxicity against human umbilical vein endothelial cells, and the Irinotecan loaded BSA beads showed comparable cytotoxicity against Hep G2, a human liver carcinoma cell line, as the traditional Irinotecan. In a rabbit model, it was found that BSA beads can successfully be transferred to liver and provide occlusion of small arteries. The present investigation suggested that the BSA beads are promising drug carriers and can potentially be used as temporary embolization agents in interventional oncology.

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.

PEGylation of bovine serum albumin using click chemistry for the application as drug carriers

2012 ◽  
Vol 28 (3) ◽  
pp. 856-861 ◽  
Author(s):  
Xiao-Yuan Li ◽  
Tai-Hang Li ◽  
Jin-Shan Guo ◽  
Ying Wei ◽  
Xia-Bin Jing ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Click Chemistry ◽  
Bovine Serum ◽  
Drug Carriers

scholarly journals FTIR Characterization and Release of Bovine Serum Albumin from Bioactive Glasses

2017 ◽  
Vol 15 (4) ◽  
pp. e347-e355 ◽  
Author(s):  
Wai-Ching Liu ◽  
Blake Ballenger ◽  
Amnah Algarni ◽  
Mariano Velez ◽  
Tien-Min G. Chu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bioactive Glass ◽  
Bovine Serum ◽  
Drug Carrier ◽  
Helical Structure ◽  
Burst Release ◽  
Chitosan Coating ◽  
Degradation Rates ◽  
Percent Protein

Background Bioactive glass has attracted substantial interest in orthopedics, but it has been less explored as a drug carrier. This study investigated the bovine serum albumin (BSA) release from bioactive 13–93B0 and 13–93B3 glasses. Methods Glass disks (13–93B0 and 13–93B3; n = 5) were loaded with 4 mg of BSA and coated under different chitosan-coating conditions. The amount of BSA released in phosphate-buffered saline (PBS) was evaluated, and a degradation study was performed to find out the weight loss and pH of PBS. Secondary structures of BSA on 13–93B0 were characterized by Fourier transform infrared (FTIR) spectroscopy. Results One hundred percent protein release occurred by 24 hours for all 13–93B3 groups. However, chitosan coating delayed 100% release up to 72 hours in 13–93B0 groups. The 13–93B3 glass showed higher degradation rates than 13–93B0 regardless of chitosan-coating status. Multilayer and sandwich chitosan coatings further delayed BSA release from 13–93B0. FTIR analysis revealed that α-helical structure was the highest among all groups and significantly higher in the 2% sandwich chitosan coating group (32.0% ± 2.1%), compared with uncoated and 4% chitosan groups. Conclusions Chitosan coating can delay the burst release of BSA from 13–93B0 glass and be a potential coating on bioactive glass for drug delivery purposes.

scholarly journals High Potency of SN-38-Loaded Bovine Serum Albumin Nanoparticles Against Triple-Negative Breast Cancer

Pharmaceutics ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 569 ◽  
Author(s):  
Lin ◽  
Chuang ◽  
Cheng ◽  
Lin ◽  
Fang
Keyword(s):  
Breast Cancer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Triple Negative Breast Cancer ◽  
Bovine Serum ◽  
Triple Negative ◽  
Control Group ◽  
Burst Release ◽  
Albumin Nanoparticles ◽  
Low Efficiency

Triple-negative breast cancer (TNBC) is an aggressive type of breast cancer with a worse prognosis than other types. There are currently no specific approved treatments for TNBC. Albumin is a promising biomimetic material that may be fabricated into nanoparticles to possibly exert passive effects on targeted tumors. Irinotecan has been extensively used in clinical settings, although a high dosage is required due to its low efficiency of conversion into the active metabolite SN-38, also known as 7-ethyl-10-hydroxy-camptothecin. The aim of this work was to optimize SN-38-loaded bovine serum albumin nanoparticles (sBSANPs) and evaluate their potency against TNBC. The sBSANPs were characterized by a small size of about 134–264 nm, a negative charge of −37 to −40 mV, an entrapment efficiency of 59–71%, and a particle yield of 65–86%. The cytotoxicity assays using sBSANPs showed a higher potency specifically against both MDA-MB-468 and MDA-MB-231 cells (ER−, PR−, HER2−) compared to MCF-7 (ER+, PR+, HER2−), and exhibited an extremely low IC50 at the nanomolar levels (2.01–6.82 nM). The release profiles indicated that SN-38 presented an initial burst release within 12 h, and sBSANPs had a slow release pattern. Flow cytometry results showed that the fluorescence intensity of sBSANPs was significantly higher than that of the control group. The confocal images also confirmed that sBSANPs were taken up by MDA-MB-468 cells. Moreover, we found that a larger BSANP size resulted in an increased hemolytic effect. In vivo animal studies demonstrated that loading of SN-38 into bovine serum albumin nanoparticles could minimize the initial concentration without extending the elimination half-life, but significantly minimized the Cmax (p < 0.001) as compared with irinotecan treatment.

A Novel Thermosensitive Composite Fabricated with Au Nanoparticles, Poly(Lactide), and Poly(N-Isopropylacrylamide)

2004 ◽  
Vol 99-100 ◽  
pp. 161-164
Author(s):  
Yun Suk Jo ◽  
Do-Kyung Kim ◽  
Young Keun Jeong ◽  
Kyung Ja Kim ◽  
Mamoun Muhammed
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Au Nanoparticles ◽  
Double Emulsion ◽  
Drug Carriers ◽  
Shell Structures ◽  
Emulsion Method ◽  
Novel Approach

A novel approach to load a hydrophilic bovine serum albumin (BSA) into the drug carriers was proposed in terms of thermosensitive dual-shell structures which were fabricated with poly(N-isopropylacrylamide), poly(lactide) and Au nanoparticles. Spherically well-defined dualshell structures were constructed by a modified-double-emulsion method (MDEM). The lower critical solubility temperature of the structures was shifted to 36.4 °C which was confirmed by UVVis spectroscopy.

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

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