scispace - formally typeset
Search or ask a question

Showing papers on "Bovine serum albumin published in 2014"


Journal ArticleDOI
TL;DR: The results show that protein secondary structure is a key parameter in determining the cell surface receptor used by a protein–nanoparticle complex, and it is expected this link between protein structure and cellular outcomes will provide a molecular basis for the design of nanoparticles for use in biological and biomedical applications.
Abstract: Nanoparticles used for biological and biomedical applications encounter a host of extracellular proteins. These proteins rapidly adsorb onto the nanoparticle surface, creating a protein corona. Poly(ethylene glycol) can reduce, but not eliminate, the nonspecific adsorption of proteins. As a result, the adsorbed proteins, rather than the nanoparticle itself, determine the cellular receptors used for binding, the internalization mechanism, the intracellular transport pathway, and the subsequent immune response. Using fluorescence microscopy and flow cytometry, we first characterize a set of polystyrene nanoparticles in which the same adsorbed protein, bovine serum albumin, leads to binding to two different cell surface receptors: native albumin receptors and scavenger receptors. Using a combination of circular dichroism spectroscopy, isothermal titration calorimetry, and fluorescence spectroscopy, we demonstrate that the secondary structure of the adsorbed bovine serum albumin protein controls the cellular ...

183 citations


Journal ArticleDOI
TL;DR: The protein size was found to be a critical factor for the photostability and long-term stability of gold nanoclusters and the size of the protein also affected the Au nanocluster behaviour after immobilization.
Abstract: Protein-encapsulated gold nanoclusters have shown many advantages over other gold nanocluster systems, including green synthesis, biocompatibility, high water solubility, and the ease of further conjugation. In this article, we systematically investigated the effects of the protein size and amino acid content on the formation and fluorescent properties of gold nanoclusters using four model proteins (bovine serum albumin, lysozyme, trypsin, and pepsin). We discovered that the balance of amine and tyrosine/tryptophan containing residues was critical for the nanocluster formation. Protein templates with low cysteine contents caused blue shifts in the fluorescent emissions and difference in fluorescent lifetimes of the gold nanoclusters. Furthermore, the protein size was found to be a critical factor for the photostability and long-term stability of gold nanoclusters. The size of the protein also affected the Au nanocluster behaviour after immobilization.

170 citations


Journal ArticleDOI
01 Sep 2014-Peptides
TL;DR: The use of in silico methodologies, peptide databases and software to assess the release of potentially bioactive DPP-IV, renin and ACE-I inhibitory peptides from bovine and porcine meat proteins demonstrating that meat proteins are a suitable resource for the generation of bioactive peptides is demonstrated.

133 citations


Journal ArticleDOI
12 Nov 2014
TL;DR: The aim of this review is to focus on the structure and biological functions of bovine serum albumin, the design of metal complexes that are able to bind to the biomolecule, as well as the experimental techniques employed in the study and evaluation of these interactions.
Abstract: The continuous search for new molecules with therapeutic abilities has led to the synthesis and characterization of a large number of metal complexes, proven to exhibit potential as pharmacological agents through their antibacterial, antiviral, antifungal and antineoplastic properties. As serum albumins play a key role in drug pharmacokinetics and pharmacodynamics, the study of coordination compounds affinity towards this class of proteins, as well as understanding the mechanism through which they interact is crucial. The aim of this review is to focus on the structure and biological functions of bovine serum albumin, the design of metal complexes that are able to bind to the biomolecule, as well as the experimental techniques employed in the study and evaluation of these interactions.

125 citations


Journal ArticleDOI
01 Sep 2014-Proteins
TL;DR: A comparison of the structurally investigated complexes with the analogous complex of human serum albumin (HSA‐NPS) revealed surprising differences in the number and distribution of naproxen binding sites.
Abstract: Serum albumin, a protein naturally abundant in blood plasma, shows remarkable ligand binding properties of numerous endogenous and exogenous compounds. Most of serum albumin binding sites are able to interact with more than one class of ligands. Determining the protein-ligand interactions among mammalian serum albumins is essential for understanding the complexity of this transporter. We present three crystal structures of serum albumins in complexes with naproxen (NPS): bovine (BSA-NPS), equine (ESA-NPS), and leporine (LSA-NPS) determined to 2.58 A (C2), 2.42 A (P61), and 2.73 A (P212121) resolutions, respectively. A comparison of the structurally investigated complexes with the analogous complex of human serum albumin (HSA-NPS) revealed surprising differences in the number and distribution of naproxen binding sites. Bovine and leporine serum albumins possess three NPS binding sites, but ESA has only two. All three complexes of albumins studied here have two common naproxen locations, but BSA and LSA differ in the third NPS binding site. None of these binding sites coincides with the naproxen location in the HSA-NPS complex, which was obtained in the presence of other ligands besides naproxen. Even small differences in sequences of serum albumins from various species, especially in the area of the binding pockets, influence the affinity and the binding mode of naproxen to this transport protein. Proteins 2014; 82:2199–2208. © 2014 Wiley Periodicals, Inc.

121 citations


Journal ArticleDOI
TL;DR: A novel epitope molecularly imprinted polymer for specific recognition and direct fluorescent quantification of the target protein bovine serum albumin (BSA) was demonstrated where polymerization was performed on the surface of silica nanospheres embedded CdTe quantum dots (QDs).

117 citations


Journal ArticleDOI
TL;DR: It is considered that the bovine serum albumin nanoparticles may have potential applications in the field of local drug delivery in the treatment of inner ear disorders.
Abstract: Nanoparticles have attracted increasing attention for local drug delivery to the inner ear recently. Bovine serum albumin (BSA) nanoparticles were prepared by desolvation method followed by glutaraldehyde fixation or heat denaturation. The nanoparticles were spherical in shape with an average diameter of 492 nm. The heat-denatured nanoparticles had good cytocompatibility. The nanoparticles could adhere on and penetrate through the round window membrane of guinea pigs. The nanoparticles were analyzed as drug carriers to investigate the loading capacity and release behaviors. Rhodamine B was used as a model drug in this paper. Rhodamine B-loaded nanoparticles showed a controlled release profile and could be deposited on the osseous spiral lamina. We considered that the bovine serum albumin nanoparticles may have potential applications in the field of local drug delivery in the treatment of inner ear disorders.

117 citations


Journal ArticleDOI
TL;DR: The structure-function relationships are reviewed in the light of the structural state of the protein (native versus non-native aggregated proteins), and the binding properties of native β-lg (localization of binding sites, stoichiometry, and affinity) and some biological properties of the complexes are addressed.
Abstract: Ligand-binding properties of β-lactoglobulin (β-lg) are well documented, but the subsequent biological functions are still unclear. Focusing on fatty acids/β-lg complexes, the structure-function relationships are reviewed in the light of the structural state of the protein (native versus non-native aggregated proteins). After a brief description of β-lg native structure, the review takes an interest in the binding properties of native β-lg (localization of binding sites, stoichiometry, and affinity) and the way the interaction affects the biological properties of the protein and the ligand. The binding properties of non-native aggregated forms of β-lg that are classically generated during industrial processing are also related. Structural changes modify the stoichiometry and the affinity of β-lg for fatty acids and consequently the biological functions of the complex. Finally, the fatty acid-binding properties of other whey proteins (α-lactalbumin, bovine serum albumin) and some biological properties of the complexes are also addressed. These proteins affect β-lg/fatty acids complex in whey given their competition with β-lg for fatty acids.

113 citations


Journal ArticleDOI
TL;DR: It is shown that by addition of bovine serum albumin, the toxicity of nanoparticles is greatly reduced and the drug-loaded system exhibited excellent therapeutic potential in vitro, exceeding that of free mitoxantrone.
Abstract: The promising potential of superparamagnetic iron oxide nanoparticles (SPIONs) in various nanomedical applications has been frequently reported. However, although many different synthesis methods, coatings, and functionalization techniques have been described, not many core-shell SPION drug delivery systems are available for clinicians at the moment. Here, bovine serum albumin was adsorbed onto lauric acid-stabilized SPIONs. The agglomeration behavior, zeta potential, and their dependence on the synthesis conditions were characterized with dynamic light scattering. The existence and composition of the core-shell-matrix structure was investigated by transmission electron microscopy, Fourier transform infrared spectroscopy, and zeta potential measurements. We showed that the iron oxide cores form agglomerates in the range of 80 nm. Moreover, despite their remarkably low tendency to aggregate even in a complex media like whole blood, the SPIONs still maintained their magnetic properties and were well attractable with a magnet. The magnetic properties were quantified by vibrating sample magnetometry and a superconducting quantum interference device. Using flow cytometry, we further investigated the effects of the different types of nanoparticle coating on morphology, viability, and DNA integrity of Jurkat cells. We showed that by addition of bovine serum albumin, the toxicity of nanoparticles is greatly reduced. We also investigated the effect of the particles on the growth of primary human endothelial cells to further demonstrate the biocompatibility of the particles. As proof of principle, we showed that the hybrid-coated particles are able to carry payloads of up to 800 μg/mL of the cytostatic drug mitoxantrone while still staying colloidally stable. The drug-loaded system exhibited excellent therapeutic potential in vitro, exceeding that of free mitoxantrone. In conclusion, we have synthesized a biocompatible ferrofluid that shows great potential for clinical application. The synthesis is straightforward and reproducible and thus easily translatable into a good manufacturing practice environment.

111 citations


Journal ArticleDOI
Jianfeng Han1, Qin Wang1, Zhirong Zhang1, Tao Gong1, Xun Sun1 
01 Feb 2014-Small
TL;DR: Results indicate that CBSA-based self-assembled nanoparticles can be a promising strategy for a siRNA delivery system for lung targeting and metastatic cancer therapy.
Abstract: It is generally believed that intravenous application of cationic vectors is limited by the binding of abundant negatively charged serum components, which may cause rapid clearance of the therapeutic agent from the blood stream. However, previous studies show that systemic delivery of cationic gene vectors mediates specific and efficient transfection within the lung, mainly as a result of interaction of the vectors with serum proteins. Based on these findings, a novel and charge-density-controllable siRNA delivery system is developed to treat lung metastatic cancer by using cationic bovine serum albumin (CBSA) as the gene vector. By surface modification of BSA, CBSA with different isoelectric points (pI) is synthesized and the optimal cationization degree of CBSA is determined by considering the siRNA binding and delivery ability, as well as toxicity. The CBSA can form stable nanosized particles with siRNA and protect siRNA from degradation. CBSA also shows excellent abilities to intracellularly deliver siRNA and mediate significant accumulation in the lung. When Bcl2-specific siRNA is introduced to this system, CBSA/siRNA nanoparticles exhibit an efficient gene-silencing effect that induces notable cancer cell apoptosis and subsequently inhibits the tumor growth in a B16 lung metastasis model. These results indicate that CBSA-based self-assembled nanoparticles can be a promising strategy for a siRNA delivery system for lung targeting and metastatic cancer therapy.

110 citations


Journal ArticleDOI
Zhe Gao1, Ilya Zharov1
TL;DR: A one-pot synthesis of large-pore mesoporous silica nanoparticles using a nonsurfactant template, tannic acid, and protein immobilization on these particles is described in this paper.
Abstract: We describe a one-pot synthesis of novel large-pore mesoporous silica nanoparticles using a nonsurfactant template, tannic acid, and protein immobilization on these particles. The tannic-acid-templated mesoporous silica nanoparticles (TA-MSNPs) possess tunable large pores (6–13 nm), unique pore morphology, and a uniform diameter of ca. 200 nm. TA-MSNPs show high protein adsorption capacity of 77.1 mg/g for lysozyme, 396.5 mg/g for bovine hemoglobin, and 130.0 mg/g for bovine serum albumin and rapid protein uptake. They can also adsorb a large amount of m-MDH (421 ± 13 mg/g) and protect this enzyme from the environment, as demonstrated by its high activity when encapsulated inside the mesopores of TA-MSNPs.

Journal ArticleDOI
TL;DR: A model whereby the electrophoretic motion of the proteins leads to a frictional force that results in protein unfolding is proposed, which is a critical initial step for protein aggregation and potentially amyloid fibril formation.
Abstract: The effect of a low strength oscillating electric field on the conformation of Bovine Serum Albumin (BSA) and Lysozyme in solution has been measured. A purpose built cell has been used to measure the real time autofluorescence and Circular Dichroism of the protein solutions exposed to electric fields of differing strength and frequency. Exposure to the electric fields results in protein unfolding for both Lysozyme and BSA. The applied field strengths are extremely small compared to the protein inter-chain intra-molecular forces. We propose a model whereby the electrophoretic motion of the proteins leads to a frictional force that results in protein unfolding. For BSA and Lysozyme in the electric fields used in this study, the shear rates at the protein surface under electrophoretic motion are of order 10(3) and 10(4) s(-1) respectively. Prolonged electric field exposure results in significant frictional energy dissipation in the proteins. The energy dissipated in the proteins results in protein unfolding, which is a critical initial step for protein aggregation and potentially amyloid fibril formation.

Journal ArticleDOI
TL;DR: Owning to the protection effect of the protein shell, BSA-PtNPs turn out to be very stable and preserve the catalytic activity in the presence of protein and even in the real plasma samples, making them suitable for a wide range of applications in sensors for biological samples.

Journal ArticleDOI
TL;DR: Lf-NPs were a prospective dual-targeting drug delivery system for effective targeting therapy of brain gliomas and showed the strongest cytotoxicity and the highest effectiveness in the uptake both in BCECs and C6 as well as improved the dual- targeting effects.
Abstract: In this study, a dual-targeting drug delivery system based on bovine serum albumin nanoparticles (BSA-NPs) modified with both lactoferrin (Lf) and mPEG2000 loading doxorubicin (DOX) was designed, and its blood–brain barrier (BBB) penetration and brain glioma cells targeting properties were explored. BSA-NPs were prepared by a desolvation technique, and mPEG2000 was incorporated onto the surface of BSA-NPs by reacting with the free amino-group of BSA to form mPEG2000-modified BSA-NPs (P2000-NPs). Finally, Lf-modified P2000-NPs (Lf-NPs) was obtained by absorbing Lf onto the surface of P2000-NPs via the positive and negative charges interaction at physiological pH. Three levels of mPEG2000 and Lf-modified NPs were prepared and characterized, respectively. The uptake and potential cytotoxicity of different DOX preparations in vitro by the primary brain capillary endothelial cells (BCECs) and glioma cells (C6) were investigated. The dual-targeting effects were studied on the BBB model in vitro, BCECs/C6 glioma...

Journal ArticleDOI
TL;DR: Using dynamic light scattering and transmission electron microscopy to investigate the adsorption of serum proteins on gold nanoparticles with different surface modifications showed 6–8 nm thick BSA and TRF coronas (corresponding to monolayer or bilayer proteins), in which the microscopic dissociation constants are in the range of 10−8 to 10−6 M.
Abstract: Protein coronas provide the biological identity of nanomaterials in vivo. Here we have used dynamic light scattering (DLS) and transmission electron microscopy (TEM) to investigate the adsorption of serum proteins, including bovine serum albumin (BSA), transferrin (TRF) and fibrinogen (FIB), on gold nanoparticles (AuNPs) with different surface modifications (citrate, thioglycolic acid, cysteine, polyethylene glycol (PEG, Mw = 2 k and 5 k)). AuNPs with PEG(5 k) surface modification showed no protein adsorption. AuNPs with non-PEG surface modifications showed aggregation with FIB. AuNPs with citrate and thioglycolic acid surface modifications showed 6–8 nm thick BSA and TRF coronas (corresponding to monolayer or bilayer proteins), in which the microscopic dissociation constants of BSA and TRF protein coronas are in the range of 10−8 to 10−6 M. Open image in new window

Journal ArticleDOI
TL;DR: In insights for the design of surface active ILs for protein stabilization as a potential replacement for the mixed micelles of conventional surfactants used in detergent industries for enzyme stabilization and as an artificial chaperone, [C8mim][C12OSO3] stabilizes BSA against the aggregation which is the major cause of protein destabilization.
Abstract: 3-Methyl-1-octylimidazolium dodecylsulfate, [C8mim][C12OSO3], a vesicle forming biamphiphilic ionic liquid (BAIL) (J. Phys. Chem. B 2012, 116, 14363-14374), has been found to induce significant folding alterations in the structure of bovine serum albumin (BSA) in the aqueous medium at pH 7.0. Such alterations have been investigated in detail using various physicochemical and spectroscopic techniques. Different concentration regimes (monomeric, shared aggregation, and post-vesicular) of [C8mim][C12OSO3]-BSA interactions have been defined through adsorption and binding isotherms using tensiometry and isothermal titration calorimetry (ITC). Fluorimetry, circular dichroism (CD), and dynamic light scattering (DLS) measurements have shown that [C8mim][C12OSO3] induces a small unfolding of BSA in the monomeric regime at low concentration (designated as C(f)), which is followed by a refolding up to critical aggregation concentration (CAC) (designated as C1). Above C1, i.e., in the shared aggregation concentration regime, again a small unfolding of BSA was observed up to critical vesicular concentration (CVC) (designated as C2). In the vesicular and post-vesicular regimes, the BSA remained stable against folding alterations. The kinetic stability of BSA in the vesicular concentration regimes was studied for a month using turbidimetry. It has been found that [C8mim][C12OSO3] stabilizes BSA against the aggregation which is the major cause of protein destabilization. The present study gives insights for the design of surface active ILs for protein stabilization as a potential replacement for the mixed micelles of conventional surfactants used in detergent industries for enzyme stabilization and as an artificial chaperone.

Journal ArticleDOI
TL;DR: In this article, the interaction between p-nitrophenol (PNP) and bovine serum albumin (BSA) was investigated by fluorescence quenching, UV-visible absorption, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy under the simulative physiological conditions.

Journal ArticleDOI
TL;DR: The zinc(II) complex of the non-steroidal anti-inflammatory drug tolfenamic acid in the presence of 2,2'-dipyridylketone oxime as a N,N'-donor heterocyclic ligand has been synthesized and characterized by physicochemical techniques including X-ray crystallography.

Journal ArticleDOI
TL;DR: Comparisons with prior results for the polycation poly(diallyldimethylammonium chloride) (PDADMAC) show reversal of protein selectivity due to reversal of the polyelectrolyte charge, may be related to the higher chain flexibility and effective linear charge density of this polycation.

Journal ArticleDOI
TL;DR: It is demonstrated that astringent perception is likely to increase with increasing polymer size, and further research to expand the understanding of astringents perception and its correlation with protein precipitation would benefit from sensory analysis of condensed tannins across a range of polymer sizes.

Journal ArticleDOI
TL;DR: The chlorogenate oxidovanadium complex behaved as good antioxidant agent with strongest inhibitory effects on O2(-, OH and ROO radicals and exhibited selective cytotoxicity against SKBR3 cancer cell line.

Journal ArticleDOI
TL;DR: DNA cleavage experiments indicate that the complexes exhibit efficient DNA cleavage activities without any external agents, and hydroxyl radical (HO) and singlet oxygen ((1)O2) may serve as the major cleavage active species.

Journal ArticleDOI
TL;DR: The emission titration experiments between HSA/BSA and TBO revealed the existence of strong interactions between TBO and the proteins, and the primary binding site of TBO is located in site I of HSA /BSA involving hydrophobic, hydrogen bonding and electrostatic interaction.

Journal ArticleDOI
TL;DR: The kinetics of the glycoxidation of bovine serum albumin as a model protein by three sugars is compared using fluorometric measurements of the content of advanced glycation end products (AGEs), protein-bound fructosamine, dityrosine, N'-formylkynurenines, kynurenine, tryptophan, as well as thiol groups.
Abstract: The aim of this study was to compare the kinetics of the glycoxidation of bovine serum albumin (BSA) as a model protein by three sugars: glucose, fructose and ribose, using fluorometric measurements of the content of advanced glycation end products (AGEs), protein-bound fructosamine, dityrosine, N'-formylkynurenine, kynurenine, tryptophan, the content of advanced oxidation protein products (AOPP), protein carbonyl groups, as well as thiol groups. Moreover, the levels of glycoalbumin and AGEs were determined by using an enzyme-linked immunosorbent assay. Based on the kinetic results, the optimal incubation time for studies of the modification of the glycoxidation rate by additives was chosen, and the effects of 25 compounds of natural origin on the glycoxidation of BSA induced by various sugars were examined. The same compounds were found to have different effects on glycoxidation induced by various sugars, which suggests caution in extrapolation from experiments based on one sugar to other sugars. From among the compounds tested, the most effective inhibitors of glycoxidation were: polyphenols, pyridoxine and 1-cyano-4-hydroxycinnamic acid.

Journal ArticleDOI
Jing Wang1, Wei Wu1, Yajun Zhang1, Xin Wang1, Hanqing Qian1, Baorui Liu1, Xiqun Jiang1 
TL;DR: It is demonstrated that the drug accumulation and particle residence time at tumor site can be significantly improved by incorporating boronic acid group into the bovine serum albumin nanoparticles, optimizing particle size and decorating particle surface.

Journal ArticleDOI
TL;DR: Flow cytometry analysis reveals that 1 mediates the arrest of S and G2/M phases in the cell cycle progression at 24h harvesting time, which progresses into apoptosis, and hoechst 33258 staining studies indicate the higher potency of 1 to induce apoptosis.

Journal ArticleDOI
TL;DR: Molecular docking studies utilizing oxovanadium(IV)-salphen derivatives show strong binding with BSA and give insight into the binding modes, interaction pattern and stability of synthesized complexes in the target site and the cytotoxicity study shows the ability of these V(IV) complexes to inhibit the growth of AGS gastric cell lines.
Abstract: Vanadyl compounds of clinical significance are recommended as drugs against diseases such as tuberculosis, diabetes, cancer, etc. In order to check the potential of the salphen ligands and oxovanadium(IV)–salphen complexes as drugs their binding with bovine serum albumin (BSA) is investigated. The binding constants measured at pH 7.4 using UV-vis absorption and fluorescence techniques are in the range of 103–105 M−1. The quenching of the fluorescence of BSA and appearance of enhanced luminescence of the salphen ligand/vanadium(IV) complex at the increased [quencher] show efficient FRET from the protein to the quencher and the distance of energy transfer estimated using Forster's theory is in the range of 1.4–3.5 nm. Molecular docking studies (DFT) utilizing oxovanadium(IV)–salphen derivatives show strong binding with BSA and give insight into the binding modes, interaction pattern and stability of synthesized complexes in the target site. The cytotoxicity study shows the ability of these V(IV) complexes to inhibit the growth of AGS gastric cell lines.

Journal ArticleDOI
TL;DR: The results show that sdAb-functionalized particles can effectively target the EGFR, even in more complex bovine and human serum conditions where targeting specificity is largely conserved for increasing serum concentration.
Abstract: For effective localization of functionalized nanoparticles at diseased tissues such as solid tumours or metastases through biorecognition, appropriate targeting vectors directed against selected tumour biomarkers are a key prerequisite. The diversity of such vector molecules ranges from proteins, including antibodies and fragments thereof, through aptamers and glycans to short peptides and small molecules. Here, we analyse the specific nanoparticle targeting capabilities of two previously suggested peptides (D4 and GE11) and a small camelid single-domain antibody (sdAb), representing potential recognition agents for the epidermal growth factor receptor (EGFR). We investigate specificity by way of receptor RNA silencing techniques and look at increasing complexity in vitro by introducing increasing concentrations of human or bovine serum. Peptides D4 and GE11 proved problematic to employ and conjugation resulted in non-receptor specific uptake into cells. Our results show that sdAb-functionalized particles can effectively target the EGFR, even in more complex bovine and human serum conditions where targeting specificity is largely conserved for increasing serum concentration. In human serum however, an inhibition of overall nanoparticle uptake is observed with increasing protein concentration. For highly affine targeting ligands such as sdAbs, targeting a receptor such as EGFR with low serum competitor abundance, receptor recognition function can still be partially realised in complex conditions. Here, we stress the value of evaluating the targeting efficiency of nanoparticle constructs in realistic biological milieu, prior to more extensive in vivo studies.

Journal ArticleDOI
Xueqin Ding1, Yuzhi Wang1, Qun Zeng1, Jing Chen1, Yanhua Huang1, Kaijia Xu1 
TL;DR: The proposed FGIL-ATPS has been applied to purify lysozyme, trypsin, ovalbumin and bovine serum albumin and shows that it has huge potential to offer new possibility in the purification of proteins.

Journal ArticleDOI
Rui Yang1, Yanli An, Fengqin Miao1, Mengfei Li1, Peidang Liu1, Qiusha Tang1 
TL;DR: Folic acid-conjugated bovine serum albumin nanospheres composed of mixed doxorubicin and magnetic iron oxide cores can enable controlled and targeted delivery of anticancer drugs and may offer a promising alternative to targeted doxorbicin therapy for nasopharyngeal carcinoma.
Abstract: Background: This study aimed to generate targeted folic acid-conjugated, doxorubicin-loaded, magnetic iron oxide bovine serum albumin nanospheres (FA-DOX-BSA MNPs) that lower the side effects and improve the therapeutic effect of antitumor drugs when combined with hyperthermia and targeting therapy. A new nanodrug using magnetic nanospheres for heating and addition of the folate receptor with cancer cell specificity was prepared. The characteristics of these nanospheres and their antitumor effects in nasopharyngeal carcinoma were explored. Methods: FA-DOX-BSA MNPs comprising encapsulated magnetic iron oxide nanoparticles were prepared using a desolvation cross-linking method. Activated folic acid (Nhydroxysuccinimide ester of folic acid) was conjugated to the surface of albumin nanospheres via amino groups. Results: Folic acid was successfully expressed on the surface of the nanospheres. Electron microscopy revealed that the FA-DOX-BSA MNPs were nearly spherical and uniform in size, with an average diameter of 180 nm. The nanomaterial could deliver doxorubicin at clinically relevant doses with an entrapment efficiency of 80%. An increasing temperature test revealed that incorporation of magnetic iron oxide into nanospheres could achieve a satisfactory heat treatment temperature at a significantly lower dose when placed in a high-frequency alternating magnetic field. FA-DOX-BSA MNPs showed greater inhibition of tumors than in the absence of folic acid in vitro and in vivo. Compared with chemotherapy alone, hyperthermia combined with chemotherapy was more effective against tumor cells. Conclusion: Folic acid-conjugated bovine serum albumin nanospheres composed of mixed doxorubicin and magnetic iron oxide cores can enable controlled and targeted delivery of anticancer drugs and may offer a promising alternative to targeted doxorubicin therapy for nasopharyngeal carcinoma.