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.

Exploring the interaction of l-cysteine capped CuS nanoparticles with bovine serum albumin (BSA): a spectroscopic study

RSC Advances ◽  
2016 ◽  
Vol 6 (63) ◽  
pp. 58288-58295 ◽  
Author(s):  
S. Prasanth ◽  
D. Rithesh Raj ◽  
T. V. Vineeshkumar ◽  
Riju K. Thomas ◽  
C. Sudarsanakumar
Keyword(s):  
Particle Size ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Copper Sulfide ◽  
Average Particle Size ◽  
Precipitation Method ◽  
Average Particle ◽  
Spectroscopic Techniques ◽  
Co Precipitation

l-Cysteine capped copper sulfide nanoparticles with an average particle size of 6 nm were synthesized using a chemical co-precipitation method and their interactions with bovine serum albumin were explored using various spectroscopic techniques.

scholarly journals Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

Materials ◽  
2021 ◽  
Vol 14 (2) ◽  
pp. 298
Author(s):  
Shufang Liu ◽  
Shu’e Wang ◽  
Zhanzuo Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Inner Filter Effect ◽  
Spectroscopic Techniques ◽  
Size Distributions ◽  
Size Dependent ◽  
Filter Effect ◽  
Vis Spectroscopy

The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.

Monitoring the interactions between bovine serum albumin and ZnO/Ag nanoparticles by spectroscopic techniques

2021 ◽  
pp. 1-14
Author(s):  
Abhishek Udnoor ◽  
Manjunath Lokolkar ◽  
Basappa C. Yallur ◽  
Raju Kale ◽  
Muttanagoud N. Kalasad ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ag Nanoparticles ◽  
Bovine Serum ◽  
Spectroscopic Techniques

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.

Study of the interaction between doxepin hydrochloride and bovine serum albumin by spectroscopic techniques

2006 ◽  
Vol 39 (4-5) ◽  
pp. 234-239 ◽  
Author(s):  
P.B. Kandagal ◽  
J. Seetharamappa ◽  
S. Ashoka ◽  
S.M.T. Shaikh ◽  
D.H. Manjunatha
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Techniques

Interaction between carisoprodol and bovine serum albumin and effect of β-cyclodextrin on binding: insights from molecular docking and spectroscopic techniques

RSC Advances ◽  
2016 ◽  
Vol 6 (68) ◽  
pp. 63463-63471 ◽  
Author(s):  
Mallavva B. Bolattin ◽  
Sharanappa T. Nandibewoor ◽  
Shrinivas D. Joshi ◽  
Sheshagiri R. Dixit ◽  
Shivamurti A. Chimatadar
Keyword(s):  
Amino Acids ◽  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Techniques ◽  
Hydrophobic Amino Acids

Interactions between the BSA and CAP in the docked model. Figure showing H-bonding interactions and carisoprodol surrounded by hydrophobic amino acids Leu249, Leu250 and Gly247 in subdomain IIA.

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