Bovine Serum Albumin as a Versatile Platform for Cancer Imaging and Therapy

Background: Due to the good biocompatibility, biodegradability, facile surface functionalization and high water solubility, Bovine serum albumin has gain increasing attention in the nanomedicine. Objective: Despite there are many reviews on albumin based nanoparticles, most of them focus on one aspect of the albumin functionality, e.g., drug delivery, cancer theranostics or half-life extension in vivo. This review aims to comprehensively summary bovine serum albumin as a versatile platform in the applications of cancer imaging and therapy. Methods: We review the extensive applications of bovine serum albumin in drug carrier, surface engineering and biomimetic synthesis for cancer imaging and therapy. Conclusion: Based on the studies reviewed, variety of in vitro and in vivo studies show good performance of bovine serum albumin as the drug carrier, surface modification agent and biomimetic template in cancer imaging and therapy. Nevertheless, there are still some issues to be solved, e.g., the technological parameters for enhancing the drug loading efficiency and controlling drug release, optimizing surface modification process to provide more stable nanoagents, investigation of the biomimetic mechanism, in-depth study of their toxicity, further exploring their bioapplications, etc.

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PREPARATION OF FOLATE-CONJUGATED BOVINE SERUM ALBUMIN NANOPARTICLES ADSORBING EPIRUBICIN HYDROCHLORIDE

NANO ◽

10.1142/s1793292013500665 ◽

2013 ◽

Vol 08 (06) ◽

pp. 1350066 ◽

Cited By ~ 1

Author(s):

XIUHUA ZHAO ◽

JIAMING TANG ◽

YUANGANG ZU ◽

WEIGUO WANG ◽

NA LI ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Drug Carrier ◽

Drug Loading ◽

Carrier System ◽

Adsorption Time ◽

Inhibitory Rate ◽

Albumin Nanoparticles ◽

Drug Carrier System

This work investigated the preparation process of folate-conjugated bovine serum albumin nanoparticles (FA–BSANPs) adsorbing epirubicin hydrochloride (EPI) nanoparticles (FA–EPI–BSANPs), a specific-targeting drug delivery system in cancer chemotherapy. The BSANPs were prepared by desolvation as a drug carrier system and conjugated with folate to produce FA–EPI–BSANPs that specifically target tumors by cross-linking. EPI, an anticancer drug, was adsorbed by this drug carrier system. The influences of six experimental parameters, namely, the adsorption time, FA–BSANPs solution-adsorbed EPI concentration, stirring speed, FA–BSANPs solution pH, the ratio of glutaraldehyde and BSA, and mass ratio of FA–BSANPs to EPI, on the drug loading efficiency (DLR) and drug entrapment efficiency (DER) of FA–EPI–BSANPs were investigated via the single factor method. The results indicated that the optimum operation conditions were obtained with 145.4 nm±0.5 nm MPS, 23.41% DLR and 98.93% DER. The N -hydroxysuccinimide-folate content associated with BSANPs was up to 0.9757% (wt). The DLR and DER of EPI increased with increasing adsorption time, FA–BSANPs solution concentration, and pH value, peaking at 1750 rpm with increasing stirring speed, but decreasing thereafter. The FA–EPI–BSANPs obtained were characterized by laser light scattering, scanning electron microscopy, Fourier transform infrared spectroscopy, differential scanning calorimetry, X-ray diffraction and thermogravimetric analysis. Drug release in vitro was investigated, as well. The characterization results showed that EPI in FA–EPI–BSANPs existed in an amorphous, instead of crystalline state. Most of the EPI was enclosed by FA–BSANPs, and a small amount was adsorbed onto the surface of the FA–BSANPs. The FA–EPI–BSANPs particles are nearly ellipsoidal and significantly affect sustained release. The inhibitory rate of FA–EPI–BSANP was mensurated by MTT method. The inhibitory rate of FA–EPI–BSANPs for SMMC 7721 cell developed with raise of concentration and was higher than other samples. The IC50 values of FA–EPI–BSANPs and EPI were 11.5 μg/mL and 18.8 μg/mL, respectively. The target ability of FA–EPI–BSANP for SMMC 7721 cell was mensurated by fluorescence (FITC) modified albumin techniques. The uptake rate of FA–EPI–BSANPs was higher than samples without folate conjugated, and increased with increased concentration.

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Bovine serum albumin/chitosan-nanoparticle bio-complex; spectroscopic study and in vivo toxicological – Hypersensitivity evaluation

Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy ◽

10.1016/j.saa.2021.119582 ◽

2021 ◽

Vol 253 ◽

pp. 119582

Author(s):

Moataz M. Rashad ◽

Nesma M. El-Kemary ◽

Said Amer ◽

Maged El-Kemary

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Spectroscopic Study ◽

Bovine Serum ◽

Chitosan Nanoparticle

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

Dalton Transactions ◽

10.1039/d1dt00777g ◽

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...

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

Analytical Methods ◽

10.1039/c7ay00270j ◽

2017 ◽

Vol 9 (21) ◽

pp. 3099-3104 ◽

Cited By ~ 7

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.

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Engineering near-infrared fluorescent styrene-terminated porous silicon nanocomposites with bovine serum albumin encapsulation for in vivo imaging

Journal of Materials Chemistry B ◽

10.1039/c4tb01209g ◽

2014 ◽

Vol 2 (47) ◽

pp. 8314-8320 ◽

Cited By ~ 9

Author(s):

Bing Xia ◽

Bin Wang ◽

Jisen Shi ◽

Wenyi Zhang ◽

Shou-jun Xiao

Keyword(s):

Porous Silicon ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

In Vivo Imaging ◽

Bovine Serum ◽

Near Infrared

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Clearance and binding of native and defucosylated lactoferrin

Biochemical Journal ◽

10.1042/bj2120249 ◽

1983 ◽

Vol 212 (2) ◽

pp. 249-257 ◽

Cited By ~ 20

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.

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

Nanomedicine ◽

10.2217/nnm-2021-0195 ◽

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

Journal of Cell Science ◽

10.1242/jcs.103.2.565 ◽

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).

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