|Year : 2021 | Volume
| Issue : 3 | Page : 335-341
A modified method for the production of stable surface-functionalized bovine serum albumin nanoparticles
Abhishek Srivastava1, Anjali Prajapati1, Panchanan Pramanik1, Vinay Kumar Singh2
1 Department of Chemistry, GLA University, Lucknow, Uttar Pradesh, India
2 Department of Chemistry, Dr. Shakuntala Misra National Rehabilitation University, Lucknow, Uttar Pradesh, India
|Date of Submission||24-Jun-2021|
|Date of Acceptance||10-Aug-2021|
|Date of Web Publication||7-Sep-2021|
Department of Chemistry, GLA University, Mathura - 281 004, Uttar Pradesh
Source of Support: None, Conflict of Interest: None
Background: To enhance the therapeutic index of drugs, various targeted drug delivery systems have been developed in recent decades. Among different drug carrier systems, albumin-based nanocarriers have acquired much attention due to its nonimmunogenic, biodegradable, biocompatible, and nontoxic nature. The present investigation deals with the development of a stable carboxyl functionalized bovine serum albumin (FBSA) nanoparticles through surface modification with chloroacetic acid. Methods: FBSA nanoparticles were synthesized by ground dispersion using ethanol as a desolvating agent; the stabilization of nanoparticles was done by glutaraldehyde. Various process modalities, namely glutaraldehyde concentration, FBSA concentration, pH, ethanol addition rate, and agitation speed, were tested to obtain stable nanoparticles of suitable size. Results: The nanoparticles of average diameter 100–120 nm with − 30 mV zeta potential and 0.1 polydispersity index were obtained in neutral and alkaline medium. Particle size and surface charge are very less influenced by varying the FBSA in 10–200 mg/ml concentration range. pH of the medium strongly influences the surface charge and particle diameter of the FBSA nanoparticles. No significant effect on particle diameter was noticed on varying the ethanol addition rate, stirring rate, and glutaraldehyde amount in the studied range. The scanning electron microscopy monochrome image and dynamic light scattering image of FBSA display that nanoparticles are of around 100 nm size. Conclusions: The present study proposes the preparation of more stable bovine serum albumin nanoparticles through surface modification. The synthesized nanoparticles will be capable to deliver the cancer drugs more effectively to the targeted tumor site.
Keywords: Bovine serum albumin, desolvation process, drug delivery, nanoparticles, surface modification
|How to cite this article:|
Srivastava A, Prajapati A, Pramanik P, Singh VK. A modified method for the production of stable surface-functionalized bovine serum albumin nanoparticles. Biomed Biotechnol Res J 2021;5:335-41
|How to cite this URL:|
Srivastava A, Prajapati A, Pramanik P, Singh VK. A modified method for the production of stable surface-functionalized bovine serum albumin nanoparticles. Biomed Biotechnol Res J [serial online] 2021 [cited 2021 Nov 26];5:335-41. Available from: https://www.bmbtrj.org/text.asp?2021/5/3/335/325608
| Introduction|| |
Cancer, a group of diseases, is recognized as one of the principal causes of mortality around the world. Radiation therapy, chemotherapy, and surgery are the modalities commonly used for the treatments of cancer.,,, Toxicity and low drug availability in the action area are major problems with chemotherapy. A targeted drug delivery vehicle with biocompatibility can effectively solve major chemical concerns. Drug efficiency can be enhanced through applications aimed at nanocarrier systems.,,,,,,,,,,, Nanocarrier systems have turned out to be a vital asset in the pharmaceutical industry. Nanocarriers can bind/encapsulate/adsorb the active drug molecules and enhance their therapeutic target through targeted action and protect the drug molecule from the unwanted response of metabolism and biodegradation. Nontoxicity, ease of purification, biodegradability, and high water solubility make the albumin an ideal candidate for fabrication of nanoparticles and multifunctional drug carrier that can be conveniently given by injection.,,,
The different methods accepted for the preparation of albumin nanoparticles have relative merits. Desolvation technique is much more advantageous over other known processes for the synthesis of protein nanoparticles as it does not require the removal of oily residue and surfactants (emulsification process)., Unlike thermal gelation, it does not require high temperature, which makes this process more useful for heat-sensitive biological compounds. Self-assembly also requires toxic chemicals for the breaking of disulfide bonds., Albumin-bound nab-technology is acknowledged to be a safe and suitable method for the preparation of protein nanoparticles loaded with lipophilic drug with high drug loading capacity.,
The drug-loaded albumin nanoparticles synthesized in a variety of ways show high drug entrapment and loading capacity also, the solubility of less water-soluble drugs is improved. Furthermore, the nanoparticles exhibit a slow and sustained release of the drug in comparison to the bare drug. Cancer cells have specific type of ligand receptors that overexpress on its surface, and the incorporation of such target-specific ligand to the albumin matrix enhances the uptake of albumin nanoparticles by cancer cells., The improved accumulation of albumin nanoparticles loaded with drugs in tumor areas increases their effectiveness against various cancer cells. Albumin nanoparticles release slowly the loaded drug in a sustained manner that reduces the adverse effects of drug and increases animal survival rate.
Albumin works as a carrier protein for steroids, thyroid hormones, and fatty acids in the blood and plays an important role for the stabilization of extracellular fluid volume.,,, Human serum albumin (HSA) helps in controlling the colloidal osmotic blood pressure and regulates blood pH. Serum albumin binds Ca (II), Zn (II), Cu (II), and Ni (II) and acts as a vehicle to transport these metals in the blood. Amino acids obtained by the disintegration of albumin provide nutrition to nearby tissues. Bovine serum albumin (BSA) or fraction V is the main plasma protein of beef cattle having 69,323 Da molecular weight and 4.7 isoelectric point. The BSA precursor protein contains 607 amino acids at full length. The precursor protein on secretion losses 18-residue signal protein from N-terminal leading to the production of 589 amino acid residual protein products., The mature BSA after cut of six amino acid residues contains 583 amino acids. Due to high ligand/drug encapsulating and binding properties, biodegradability, easy to purify and low cost, BSA has wide applications in the diagnosis of AIDS, tuberculosis, and malaria and as a vehicle for drug delivery.,, Space structure, biological properties, and chemical composition of BSA are almost the same as the HSA (76%). Although these proteins are quite similar in their composition, HSA contains one-tryptophan residues than two in BSA.
Recently, the nanoparticle application in many fields of medicine due to their specific physical and chemical properties has been developed. Albumin finds numerous applications as contrast agent, implants, biosensor, theranostic agents, etc. Nanoparticles of albumin have been developed for targeting diseases such as hepatitis C, arthritis, diabetes, and cancer. Liposome-based nanocarrier is considered very successful in the treatment of chronic inflammatory lung disease by reducing the side effect and cytotoxicity of the loaded drug. Ghanavi et al. prepared rifampin-lecithin-loaded chitosan-gelatin-loaded nanoparticles. The rifampin-loaded nanoparticles show high loading capacity with slow and sustained release of rifampin. Shahanipour et al. synthesized Fe3O4 and chitosan-loaded Fe3O4 nanoparticles, results show that the chitosan-loaded Fe3O4 nanoparticles increases the glutathione peroxidase activity.
The enhanced surface area of the nanorange structures makes them a suitable candidate for surface modification or functionalization., As the albumin molecules have amine and carboxyl groups on its surface various functionalization, enrichment and surface modifications can be done to the albumin nanoparticles by the bonding interaction between active function groups and incoming ligand. The present communication deals with the synthesis of stable surface-functionalized BSA (FBSA) nanoparticles. To obtain stable FBSA nanoparticles, several preparation conditions, namely glutaraldehyde concentration, FBSA concentration, rate of ethanol addition, agitation speed, and pH were studied.
| Methods|| |
BSA (fraction V) was procured from HiMedia. Glutaraldehyde 25%, chloroacetic acid, potassium iodide, ethanol 99%, acetic acid, and other chemicals were supplied by Merck. Double distilled water was used throughout for the preparation of all solutions. The study was scientific committee of Department of Chemistry, GLA University, Mathura,India.
Preparation of functionalized bovine serum albumin
One percent aqueous solution of BSA was prepared through sonication (2 min) and its pH was fixed at 9.0 using 0.1 N NaOH. The pH of chloroacetic acid (200 mg) containing KI (50 mg) solution maintained at 7.0 (by NaHCO3) was then added dropwise to the BSA solution with stirring at 25°C, and mixture was then heated on the water bath for 6 h at 100°C. Formed FBSA was precipitated by 10% HCl and filtered by Whatman filter paper. The precipitate thus obtained was dissolved in ammonia and reprecipitated by 10% acetic acid. Afterward, the precipitate was centrifuged at 4000 rpm and washed with cold water; the washing procedure was repeated three times to remove unreacted acid. The FBSA formed was dried under a vacuum.
Preparation of functionalized bovine serum albumin nanoparticles
Carboxyl FBSA nanoparticles were prepared at 25°C temperature by a simple desolvation process [Figure 1]. The aqueous solution of FBSA (50 mg/ml) was prepared through sonication (5 min) and 0.1 N NaOH maintained its pH. The dropwise addition of ethanol with a consistent flow rate of 1 ml/min to the aqueous solution of FBSA with a stirring rate of 550 rpm leads to the formation of a turbid solution, which indicated the formation of FBSA nanoparticles. Stabilization of the produced nanoparticles was done by chemical cross-linking using glutaraldehyde, and the stirring was continued for 6 h. The orange-brown-colored FBSA nanosuspension thus obtained was centrifuged at 15,000 rpm at 8°C for 10 min. The collected nanoparticles were lyophilized to get powdered FBSA nanoparticles. Malvern zetasizer (nano-ZS series, Malvern Instruments Ltd., Malvern, UK) with a scattering angle of 173° was used to measure average particle diameter, zeta potential, and polydispersity index (PI) at 25°C. The scanning electron microscope image recorded by Stereoscan-S360 scanning electron microscopy (SEM)-Leica Cambridge, UK, under 10 kV accelerating voltage with a 15,000 magnification exhibits that the FBSA nanoparticles display 100–200 nm size.
|Figure 1: Preparation of functionalized bovine serum albumin nanoparticles|
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| Results and Discussion|| |
Effect of functionalized bovine serum albumin concentration on particle diameter, zeta potential, and polydispersity index
To obtain favorite-sized nanoparticles, FBSA concentration was varied from 10 mg/ml to 200 mg/ml at 25°C. The influence of FBSA concentration on particle size was observed at pH 7. To the FBSA aqueous solution, the ethanol as dissolving agent was added dropwise by stirring (550 rpm) until turbidity appears. After the addition of glutaraldehyde, the stirring was continued for 6 h for complete cross-linking of nanoparticles. [Table 1] shows the average diameter, PI, and zeta potential of FBSA nanoparticles at different concentrations of FBSA. In the studied range of FBSA concentration, no appreciable change in particle size and surface charge of the FBSA nanoparticles was observed [Figure 2].
|Table 1: Effect of functionalized bovine serum albumin concentration on particle size, zeta potential, and polydispersity index preparation condition: pH: 7.0, ethanol rate: 1 ml/min, stirring rate: 550 rpm, temperature: 25°C, glutaraldehyde (8%): 120 μl, stirring time: 6 h|
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|Figure 2: Effect of functionalized bovine serum albumin concentration on particle size|
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The minimum particle diameter of 101 nm with −31.8 mV surface charge was noticed at 50 mg/ml FBSA concentration. The earlier reports on albumin also show that the particle diameter is not much affected by the albumin concentration up to a particular range. The higher protein concentration may lead to the formation of larger particles; this is due to the increased electrostatic and hydrophobic interaction between the protein particles that may result in coagulation. The present investigation and earlier reports help us to choose 50 mg/ml FBSA as a preferred condition for the fabrication of FBSA nanoparticles.
Effect of pH on particle diameter, zeta potential, and polydispersity index
The charge on the protein nanoparticles is strongly influenced by the pH. Due to electrostatic interaction, more charge (positive or negative) on nanoparticles results in smaller particle sizes. To obtain stable and suitable FBSA nanoparticles, the influence of pH on particle diameter, zeta potential, and PI was studied in the pH range of 2–10.5 [Table 2]. Results reveal that the average particle size increases with an increase in pH, reaches a maximum at pH 4.0, and then decreases up to pH 6.0, after that the no appreciable change in particle size with pH is observed [Figure 3]. The isoelectric point of BSA is 4.7, after functionalization with chloroacetic acid the isoelectric point of resulting FBSA reduced to ~4.0. Due to lower surface charge or electrical neutrality near the isoelectric point of FBSA, larger protein particles are anticipated.
|Table 2: Effect of pH on particle size, zeta potential, and polydispersity index preparation conditions: functionalized bovine serum albumin: 50 mg/ml, ethanol rate: 1 ml/min, stirring rate: 550 rpm, glutaraldehyde (8%): 120 μl, temperature: 25°C, stirring time: 6 h|
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The extremely low surface charge at pH 4.0 enhances the hydrophobic interaction among the protein molecules resulting in coagulation. Due to the positive surface charge in acidic conditions (pH 2–3), the dominance of electrostatic interaction over hydrophobic interaction results in smaller particle sizes.,,,,, In weakly acidic and alkaline conditions, the hydrogen bonding reduces the hydrophobicity of protein molecules. The enhanced negative zeta potential results in strong electrostatic repulsion among the FBSA nanoparticles in alkaline condition. The reduced hydrophobicity and strong electrostatic repulsion are responsible for the smaller particle size.
Effect of ethanol addition rate on particle diameter, zeta potential, and polydispersity index
Ethanol, a desolvating agent, was used for the preparation of FBSA nanoparticles. The dropwise addition of ethanol results in denaturation of FBSA through the breaking of the disulfide bond. After fixing the pH of aqueous FBSA solution, the effect of ethanol addition rate (0.5–8.0 ml/min) on particle size, surface charge, and PI was studied [Table 3]. No significant effect on particle diameter and the surface charge was observed on varying the ethanol addition rate in the studied range [Figure 4]. The low PI value indicates the uniformity of prepared nanoparticles. The much higher addition rate will result in larger particle diameter. The result is slightly different from the earlier reports on BSA, HSA, and EA, which shows that the ethanol addition rate of more than 1–2 ml/min produces larger nanoparticles.,
|Table 3: Effect of ethanol addition rate on particle size, zeta potential, and polydispersity index preparation conditions: functionalized bovine serum albumin: 50 mg/ml, pH: 7.0, stirring rate: 550 rpm, glutaraldehyde (8%): 120 μl, temperature: 25°C, stirring time: 6 h|
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Effect of stirring rate on particle diameter, zeta potential, and polydispersity index
The dropwise addition of ethanol results in the formation of FBSA nanoparticles by the denaturation of protein. Stirring of FBSA colloidal solution is required to reduce the possible aggregation of formed nanoparticles.,, Earlier reports show that the minimum 450 rpm stirring rate is required for the production of albumin particles in the nanorange., 250–850 rpm stirring rate with dropwise addition of ethanol to 50 mg/ml aqueous solution of FBSA at pH 7 was studied to obtain stable FBSA nanoparticles of favorite size. [Table 4] demonstrates the actual experimental conduct for the FBSA particle size, zeta potential, and PI at varying stirring rates. No significant influence on zeta potential and particle diameter of prepared FBSA nanoparticles was observed on varying the stirring rate [Figure 5]. A low stirring rate of 250 and 350 rpm also produces smaller nanoparticles, indicating the lesser aggregation of FBSA nanoparticles.
|Table 4: Effect of stirring rate on particle size zeta potential and polydispersity index preparation conditions: functionalized bovine serum albumin: 50 mg/ml, pH: 7.0, ethanol rate: 1 ml/min, glutaraldehyde: 120 μl, temperature: 25°C, stirring time: 6 h|
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Effect of cross-linker amount on particle diameter, zeta potential, and polydispersity index
Nanoparticles formed after the addition of ethanol (under stirring) are unstable and can redissolve again in water or may get aggregated. Glutaraldehyde was used as a cross-linker for the stabilization of nanoparticles. Glutaraldehyde hardens the formed nanoparticles through condensation cross-linking with the amino moieties present on the surface of albumin nanoparticles. Because of the toxicity of glutaraldehyde, it is advisable to use its minimum amount for cross-linking.,,, To study the influence of cross-linker concentration on zeta potential, particle size and PI varying concentration of glutaraldehyde (1%–10%) were used [Table 5]. Results show that 1% and 2% glutaraldehyde leads to slightly larger particle size [Figure 6], minimum particle diameter was observed with 8% of glutaraldehyde while its higher concentration results in larger particle size or even precipitation may occur.
|Table 5: Effect of cross-linker amount on particle size, zeta potential, and polydispersity index preparation conditions: functionalized bovine serum albumin: 50 mg/ml, pH: 7.0, ethanol rate: 1 ml/min, stirring rate: 550 rpm, temperature: 25°C, stirring time: 6 h|
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The SEM monochrome image [Figure 7] and dynamic light scattering (DLS) image [Figure 8] of FBSA display that nanoparticles are of approximate 100 nm sizes.
|Figure 7: Scanning electron microscopy image of functionalized bovine serum albumin nanoparticles|
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|Figure 8: Dynamic light scattering data image of functionalized bovine serum albumin nanoparticles|
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| Conclusions|| |
The present study deals with the preparation of more stable BSA nanoparticles through surface modification. To obtain stable carboxyl modified BSA particles in nanorange various process parameters, namely pH of the medium, FBSA concentration, amount of ethanol, stirring rate, and glutaraldehyde amount were studied. Particle size is very less influenced by varying the FBSA in 10–200 mg/ml concentration range with almost the same surface charge. pH strongly influences the particle diameter and zeta potential of FBSA particles, and larger particles were observed near the isoelectric point. 100–120 nm ranged FBSA nanoparticles were obtained in acidic, neutral, and alkaline medium. No significant effect on average particle diameter was observed on varying the ethanol addition rate, stirring rate, and glutaraldehyde amount in the studied range. The SEM monochrome image and DLS image of FBSA display that nanoparticles are of around 100 nm size.
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Conflicts of interest
There are no conflicts of interest.
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[Figure 1], [Figure 2], [Figure 3], [Figure 4], [Figure 5], [Figure 6], [Figure 7], [Figure 8]
[Table 1], [Table 2], [Table 3], [Table 4], [Table 5]