Bovine serum albumin (BSA or "Fraction V") is a serum albumin protein, which is extracted from blood plasma of cows.

Bovine serum albumin (BSA or "Fraction V") is a serum albumin protein, which is extracted from blood plasma of cows.

Bovine serum albumin (BSA or "Fraction V") is a serum albumin protein derived from cow blood plasma. BSA is available in powder and liquid forms for use by immunology, biochemistry, and immunology-related studies. Enzyme-linked immunosorbent assay (ELISA), Western blot & dot blot, and immunocytochemistry, which includes immunofluorescence microscopy and immunohistochemistry, are among the immunoassay uses of BSA. BSA, often derived from fetal sources, is employed as a nutritional supply in microbial and cell cultures. BSA is used in a variety of commercial areas, including agricultural biotechnology, animal breeding, marine biotechnology and aquaculture, food and beverage.

Berberine (BBR) is a naturally occurring isoquinoline alkaloid obtained from plants. It has been shown to have a variety of pharmacological effects, including anticancer action. However, due to its limited water solubility and bioavailability, it is not suitable for clinical application in cancer therapy. To address these limitations and improve treatment effectiveness, we encapsulated BBR in Bovine Serum Albumin nanoparticles (BSA NPs) using a desolvation technique in the current work. The average particle size of produced nanoparticles was 116 nm for BSA NPs and 166 nm for BBR-BSA NPs, respectively. The FESEM images of nanoparticles suggested that the nanoparticles were spherical in form and size. The drug entrapment effectiveness of produced nanoparticles was determined to be 85.65%, with a 7.78% drug loading capacity.

The production of BBR-BSA NPs and their entrapment in an amorphous state is confirmed by the FTIR spectra, XRD patterns, and thermograms of DSC and TGA. According to the stability investigations of BBR-BSA NPs, the nanoparticles were relatively stable in an aqueous solution with a pH of 7.4 and deteriorated in an acidic environment (pH 5). The produced BBR-BSA NPs were selectively hazardous to breast cancer cells and killed the cells more efficiently than pure BBR, according to in vitro cytotoxicity and Trypan blue test results. Cellular uptake tests and AO/EtBr staining indicate that BBR-BSA NPs were therapeutically more effective and improved the anticancer activity of BBR by transporting it to the target region, indicating that they might be used therapeutically. All of the aforementioned data shows that BBR-BSA NPs may emerge as a potential paradigm for breast cancer therapy.

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