Displaying publications 1 - 20 of 61 in total

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  1. A note of caution on the use of crystalline bovine albumin as a reference standard in the estimation of serum proteins
    De Witt GF
    Med J Malaya, 1965 Jun;19(4):303-5.
    PMID: 4220856
    Matched MeSH terms: Serum Albumin, Bovine*
  2. Characterization of bovine serum albumin partitioning behaviors in polymer-salt aqueous two-phase systems
    Chow YH, Yap YJ, Tan CP, Anuar MS, Tejo BA, Show PL, et al.
    J Biosci Bioeng, 2015 Jul;120(1):85-90.
    PMID: 25553974 DOI: 10.1016/j.jbiosc.2014.11.021
    In this paper, a linear relationship is proposed relating the natural logarithm of partition coefficient, ln K for protein partitioning in poly (ethylene glycol) (PEG)-phosphate aqueous two-phase system (ATPS) to the square of tie-line length (TLL(2)). This relationship provides good fits (r(2) > 0.98) to the partition of bovine serum albumin (BSA) in PEG (1450 g/mol, 2000 g/mol, 3350 g/mol, and 4000 g/mol)-phosphate ATPS with TLL of 25.0-50.0% (w/w) at pH 7.0. Results also showed that the plot of ln K against pH for BSA partitioning in the ATPS containing 33.0% (w/w) PEG1450 and 8.0% (w/w) phosphate with varied working pH between 6.0 and 9.0 exhibited a linear relationship which is in good agreement (r(2) = 0.94) with the proposed relationship, ln K = α' pH + β'. These results suggested that both the relationships proposed could be applied to correlate and elucidate the partition behavior of biomolecules in the polymer-salt ATPS. The influence of other system parameters on the partition behavior of BSA was also investigated. An optimum BSA yield of 90.80% in the top phase and K of 2.40 was achieved in an ATPS constituted with 33.0% (w/w) PEG 1450 and 8.0% (w/w) phosphate in the presence of 8.5% (w/w) sodium chloride (NaCl) at pH 9.0 for 0.3% (w/w) BSA load.
    Matched MeSH terms: Serum Albumin, Bovine/isolation & purification; Serum Albumin, Bovine/chemistry*
  3. Adsorption of Bovine Serum Albumin (BSA) at the Oil/Water Interface: A Neutron Reflection Study
    Campana M, Hosking SL, Petkov JT, Tucker IM, Webster JR, Zarbakhsh A, et al.
    Langmuir, 2015 May 26;31(20):5614-22.
    PMID: 25875917 DOI: 10.1021/acs.langmuir.5b00646
    The structure of the adsorbed protein layer at the oil/water interface is essential to the understanding of the role of proteins in emulsion stabilization, and it is important to glean the mechanistic events of protein adsorption at such buried interfaces. This article reports on a novel experimental methodology for probing protein adsorption at the buried oil/water interface. Neutron reflectivity was used with a carefully selected set of isotopic contrasts to study the adsorption of bovine serum albumin (BSA) at the hexadecane/water interface, and the results were compared to those for the air/water interface. The adsorption isotherm was determined at the isoelectric point, and the results showed that a higher degree of adsorption could be achieved at the more hydrophobic interface. The adsorbed BSA molecules formed a monolayer on the aqueous side of the interface. The molecules in this layer were partially denatured by the presence of oil, and once released from the spatial constraint by the globular framework they were free to establish more favorable interactions with the hydrophobic medium. Thus, a loose layer extending toward the oil phase was clearly observed, resulting in an overall broader interface. By analogy to the air/water interface, as the concentration of BSA increased to 1.0 mg mL(-1) a secondary layer extending toward the aqueous phase was observed, possibly resulting from the steric repulsion upon the saturation of the primary monolayer. Results clearly indicate a more compact arrangement of molecules at the oil/water interface: this must be caused by the loss of the globular structure as a consequence of the denaturing action of the hexadecane.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
  4. Electrophoretic interactions between nitrocellulose membranes and proteins: Biointerface analysis and protein adhesion properties
    Low SC, Shaimi R, Thandaithabany Y, Lim JK, Ahmad AL, Ismail A
    Colloids Surf B Biointerfaces, 2013 Oct 1;110:248-53.
    PMID: 23732801 DOI: 10.1016/j.colsurfb.2013.05.001
    Protein adsorption onto membrane surfaces is important in fields related to separation science and biomedical research. This study explored the molecular interactions between protein, bovine serum albumin (BSA), and nitrocellulose films (NC) using electrokinetic phenomena and the effects of these interactions on the streaming potential measurements for different membrane pore morphologies and pH conditions. The data were used to calculate the streaming ratios of membranes-to-proteins and to compare these values to the electrostatic or hydrophobic attachment of the protein molecules onto the NC membranes. The results showed that different pH and membrane pore morphologies contributes to different protein adsorption mechanisms. The protein adsorption was significantly reduced under conditions where the membrane and protein have like-charges due to electrostatic repulsion. At the isoelectric point (IEP) of the protein, the repulsion between the BSA and the NC membrane was at the lowest; thus, the BSA could be easily attached onto the membrane/solution interface. In this case, the protein was considered to be in a compact layer without intermolecular protein repulsions.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
  5. Bovine serum albumin: survival and osmolarity effect in bovine spermatozoa stored above freezing point
    Nang CF, Osman K, Budin SB, Ismail MI, Jaffar FH, Mohamad SF, et al.
    Andrologia, 2012 May;44 Suppl 1:447-53.
    PMID: 21806660 DOI: 10.1111/j.1439-0272.2011.01203.x
    Liquid nitrogen preservation in remote farms is a limitation. The goal of this study was to determine optimum temperature above freezing point for bovine spermatozoa preservation using bovine serum albumin (BSA) as a supplementation. Pooled semen sample from three ejaculates was subjected to various BSA concentration (1, 4, 8 and 12 mg ml(-1)), before incubation in different above freezing point temperatures (4, 25 and 37 °C). Viability assessment was carried out against time from day 0 (fresh sample) until all spermatozoa become nonviable. Optimal condition for bovine spermatozoa storage was at 4 °C with 1 mg ml(-1) BSA for almost 7 days. BSA improved bovine spermatozoa viability declining rate to 44.28% at day 4 and 57.59% at day 7 compared to control, with 80.54% and 98.57% at day 4 and 7 respectively. Increase in BSA concentration did not improve sperm viability. Our results also confirmed that there was a strong negative correlation between media osmolarity and bovine spermatozoa survival rate with r = 0.885, P < 0.0001. Bovine serum albumin helps to improve survival rate of bovine spermatozoa stored above freezing point.
    Matched MeSH terms: Serum Albumin, Bovine/physiology*
  6. Protein-binding affinity of leucaena condensed tannins of differing molecular weights
    Huang XD, Liang JB, Tan HY, Yahya R, Long R, Ho YW
    J Agric Food Chem, 2011 Oct 12;59(19):10677-82.
    PMID: 21899359 DOI: 10.1021/jf201925g
    Depending on their source, concentration, chemical structure, and molecular weight, condensed tannins (CTs) form insoluble complexes with protein, which could lead to ruminal bypass protein, benefiting animal production. In this study, CTs from Leuceana leucocephala hybrid were fractionated into five fractions by a size exclusion chromatography procedure. The molecular weights of the CT fractions were determined using Q-TOF LC-MS, and the protein-binding affinities of the respective CT fractions were determined using a protein precipitation assay with bovine serum albumin (BSA) as the standard protein. The calculated number-average molecular weights (M(n)) were 1348.6, 857.1, 730.1, 726.0, and 497.1, and b values (the b value represents the CT quantity that is needed to bind half of the maximum precipitable BSA) of the different molecular weight fractions were 0.381, 0.510, 0.580, 0.636, and 0.780 for fractions 1, 2, 3, 4, and 5, respectively. The results indicated that, in general, CTs of higher molecular weight fractions have stronger protein-binding affinity than those of lower molecular weights. However, the number of hydroxyl units within the structure of CT polymers also affects the protein-binding affinity.
    Matched MeSH terms: Serum Albumin, Bovine/metabolism
  7. Bromophenol blue binding as a probe to study urea and guanidine hydrochloride denaturation of bovine serum albumin
    Halim AA, Kadir HA, Tayyab S
    J. Biochem., 2008 Jul;144(1):33-8.
    PMID: 18344543 DOI: 10.1093/jb/mvn036
    Urea and guanidine hydrochloride (GdnHCl) denaturation of bovine serum albumin (BSA) were investigated using bromophenol blue (BPB) binding as a probe. Addition of BPB to BSA produced an absorption difference spectrum in the wavelength range, 525-675 nm with a minimum at 587 nm and a maximum at 619 nm. The magnitude of absorption difference (DeltaAbs.) at 619 nm decreased on increasing urea/GdnHCl concentration and followed the denaturation curve. The denaturation was found to be a two-state, single-step transition. The transitions started at 1.75 and 0.875 M and completed at 6.5 and 3.25 M with the mid point occurring around 4.0 and 1.5 M urea and GdnHCl concentrations, respectively. The value of free energy of stabilization, DeltaGDH2O as determined from urea and GdnHCl denaturation curves was found to be 4041 and 4602 cal/mol, respectively. Taken together, these results suggest that BPB binding can be used as a probe to study urea and GdnHCl denaturation of BSA.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
  8. Parametric Investigation of Batch Adsorption of Proteins onto Polymeric Particles
    Tan MX, Agyei D, Pan S, Danquah MK
    Curr Pharm Biotechnol, 2015;16(9):816-22.
    PMID: 26119365
    BACKGROUND: Effective bimolecular adsorption of proteins onto solid matrices is characterized by in-depth understanding of the biophysical features essential to optimize the adsorption performance.

    RESULTS: The adsorption of bovine serum albumin (BSA) onto anion-exchange Q-sepharose solid particulate support was investigated in batch adsorption experiments. Adsorption kinetics and isotherms were developed as a function of key industrially relevant parameters such as polymer loading, stirring speed, buffer pH, protein concentration and the state of protein dispersion (solid/aqueous) in order to optimize binding performance and adsorption capacity. Experimental results showed that the first order rate constant is higher at higher stirring speed, higher polymer loading, and under alkaline conditions, with a corresponding increase in equilibrium adsorption capacity. Increasing the stirring speed and using aqueous dispersion protein system increased the adsorption rate, but the maximum protein adsorption was unaffected. Regardless of the stirring speed, the adsorption capacity of the polymer was 2.8 mg/ml. However, doubling the polymer loading increased the adsorption capacity to 9.4 mg/ml.

    CONCLUSIONS: The result demonstrates that there exists a minimum amount of polymer loading required to achieve maximum protein adsorption capacity under specific process conditions.

    Matched MeSH terms: Serum Albumin, Bovine/chemistry
  9. Antifouling polyethersulfone hemodialysis membranes incorporated with poly (citric acid) polymerized multi-walled carbon nanotubes
    Abidin MNZ, Goh PS, Ismail AF, Othman MHD, Hasbullah H, Said N, et al.
    Mater Sci Eng C Mater Biol Appl, 2016 Nov 01;68:540-550.
    PMID: 27524052 DOI: 10.1016/j.msec.2016.06.039
    Poly (citric acid)-grafted-MWCNT (PCA-g-MWCNT) was incorporated as nanofiller in polyethersulfone (PES) to produce hemodialysis mixed matrix membrane (MMM). Citric acid monohydrate was polymerized onto the surface of MWCNTs by polycondensation. Neat PES membrane and PES/MWCNTs MMMs were fabricated by dry-wet spinning technique. The membranes were characterized in terms of morphology, pure water flux (PWF) and bovine serum albumin (BSA) protein rejection. The grafting yield of PCA onto MWCNTs was calculated as 149.2%. The decrease of contact angle from 77.56° to 56.06° for PES/PCA-g-MWCNTs membrane indicated the increase in surface hydrophilicity, which rendered positive impacts on the PWF and BSA rejection of the membrane. The PWF increased from 15.8Lm(-2)h(-1) to 95.36Lm(-2)h(-1) upon the incorporation of PCA-g-MWCNTs due to the attachment of abundant hydrophilic groups that present on the MWCNTs, which have improved the affinity of membrane towards the water molecules. For protein rejection, the PES/PCA-g-MWCNTs MMM rejected 95.2% of BSA whereas neat PES membrane demonstrated protein rejection of 90.2%. Compared to commercial PES hemodialysis membrane, the PES/PCA-g-MWCNTs MMMs showed less flux decline behavior and better PWF recovery ratio, suggesting that the membrane antifouling performance was improved. The incorporation of PCA-g-MWCNTs enhanced the separation features and antifouling capabilities of the PES membrane for hemodialysis application.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry
  10. Effect of Solution Properties and Operating Parameters on Needleless Electrospinning of Poly(Ethylene Oxide) Nanofibers Loaded with Bovine Serum Albumin
    Ramakrishnan R, Gimbun J, Ramakrishnan P, Ranganathan B, Reddy SMM, Shanmugam G
    Curr Drug Deliv, 2019;16(10):913-922.
    PMID: 31663478 DOI: 10.2174/1567201816666191029122445
    BACKGROUND: This paper presents the effect of solution properties and operating parameters of polyethylene oxide (PEO) based nanofiber using a wire electrode-based needleless electrospinning.

    METHODS: The feed solution was prepared using a PEO dissolved in water or a water-ethanol mixture. The PEO solution is blended with Bovine Serum Albumin protein (BSA) as a model drug to study the effect of the electrospinning process on the stability of the loaded protein. The polymer solution properties such as viscosity, surface tension, and conductivity were controlled by adjusting the solvent and salt content. The morphology and fiber size distribution of the nanofiber was analyzed using scanning electron microscopy.

    RESULTS: The results show that the issue of a beaded nanofiber can be eliminated either by increasing the solution viscosity or by the addition of salt and ethanol to the PEO-water system. The addition of salt and solvent produced a high frequency of smaller fiber diameter ranging from 100 to 150 nm. The encapsulation of BSA in PEO nanofiber was characterized by three different spectroscopy techniques (i.e. circular dichroism, Fourier transform infrared, and fluorescence) and the results showed the BSA is well encapsulated in the PEO matrix with no changes in the protein structure.

    CONCLUSION: This work may serve as a useful guide for a drug delivery industry to process a nanofiber at a large and continuous scale with a blend of drugs in nanofiber using a wire electrode electrospinning.

    Matched MeSH terms: Serum Albumin, Bovine/chemistry*
  11. Recent advancement on albumin nanoparticles in treating lung carcinoma
    Sristi, Fatima M, Sheikh A, Almalki WH, Talegaonkar S, Dubey SK, et al.
    J Drug Target, 2023 Jun;31(5):486-499.
    PMID: 37125741 DOI: 10.1080/1061186X.2023.2205609
    With the advancement of nanotechnology, many different forms of nanoparticles (NPs) are created, which specifically enhance anticancer drug delivery to tumour cells. Albumin bio-macromolecule is a flexible protein carrier for the delivery of drugs that is biodegradable, biocompatible, and non-toxic. As a result, it presents itself as an ideal material for developing nanoparticles for anticancer drug delivery. Toxicological investigations demonstrated that this novel drug delivery technique is safe for use in the human population. Furthermore, drug compatibility with the albumin nanoparticle is remarkable. The robust structure of the nanoparticle, high drug encapsulation, and customisable drug release make it a promising carrier option for the treatment of lung cancer. In this review, we summarise human serum albumin and bovine serum albumin in the targeted delivery of anticancer drugs to lung cancer cells.
    Matched MeSH terms: Serum Albumin, Bovine/chemistry
  12. Investigating membrane morphology and quantity of immobilized protein for the development of lateral flow immunoassay
    Ahmad AL, Low SC, Shukor SR, Ismail A
    J Immunoassay Immunochem, 2012 Jan;33(1):48-58.
    PMID: 22181820 DOI: 10.1080/15321819.2011.591479
    This study was aimed at gaining a quantitative understanding of the effect of protein quantity and membrane pore structure on protein immobilization. The concentration of immobilized protein was measured by staining with Ponceau S and measuring its color intensity. In this study, both membrane morphology and the quantity of deposited protein significantly influenced the quantity of protein immobilization on the membrane surface. The sharpness and intensity of the red protein spots varied depending on the membrane pore structure, indicating a dependence of protein immobilization on this factor. Membranes with smaller pores resulted in a higher color density, corresponding to enhanced protein immobilization and an increased assay sensitivity level. An increased of immobilized volume has a significant jagged outline on the protein spot but, conversely, no difference in binding capacity.
    Matched MeSH terms: Serum Albumin, Bovine/analysis*; Serum Albumin, Bovine/immunology; Serum Albumin, Bovine/chemistry
  13. In silico and BSA binding study of some new biological analogs of 1,2,4-triazolependant with azinane through microwave and conventional synthesis
    Virk NA, Rehman A, Abbasi MA, Siddiqui SZ, Ashraf A, Lateef M, et al.
    Pak J Pharm Sci, 2018 Nov;31(6 (Supplementary):2645-2654.
    PMID: 30587474
    Microwave and conventional techniques were employed to synthesize a novel array of compounds 7a-g with 1,2,4-triazole and piperidine rings having great biological importance. The microwave assisted method has a better operational scope with respect to time and yield comparative to the conventional method. 1H-NMR, 13C-NMR and IR techniques were employed to justify the structure of synthesized compounds. The antioxidant, butyrylcholinesterase inhibition and urease inhibition potential of every synthesized compound was evaluated. Every member of the synthesized series was found potent against mentioned activities. Compound 7g was the most active anti-urease agent having IC50 (μM) value 16.5±0.09 even better than the thiourea with an IC50(μM) value of 24.3±0.24. The better urease inhibition potential of 7g was also elaborated and explained by docking and bovine serum albumin (BSA) binding studies.
    Matched MeSH terms: Serum Albumin, Bovine/chemical synthesis; Serum Albumin, Bovine/metabolism*
  14. Binding Characterization of Aptamer-Drug Layered Microformulations and In Vitro Release Assessment
    Tan KX, Danquah MK, Pan S, Yon LS
    J Pharm Sci, 2019 09;108(9):2934-2941.
    PMID: 31002808 DOI: 10.1016/j.xphs.2019.03.037
    Efficient delivery of adequate active ingredients to targeted malignant cells is critical, attributing to recurrent biophysical and biochemical challenges associated with conventional pharmaceutical delivery systems. These challenges include drug leakage, low targeting capability, high systemic cytotoxicity, and poor pharmacokinetics and pharmacodynamics. Targeted delivery system is a promising development to deliver sufficient amounts of drug molecules to target cells in a controlled release pattern mode. Aptameric ligands possess unique affinity targeting capabilities which can be exploited in the design of high pay-load drug formulations to navigate active molecules to the malignant sites. This study focuses on the development of a copolymeric and multifunctional drug-loaded aptamer-conjugated poly(lactide-co-glycolic acid)-polyethylenimine (PLGA-PEI) (DPAP) delivery system, via a layer-by-layer synthesis method, using a water-in-oil-in-water double emulsion approach. The binding characteristics, targeting capability, biophysical properties, encapsulation efficiency, and drug release profile of the DPAP system were investigated under varying conditions of ionic strength, polymer composition and molecular weight (MW), and degree of PEGylation of the synthetic core. Experimental results showed increased drug release rate with increasing buffer ionic strength. DPAP particulate system obtained the highest drug release of 50% at day 9 at 1 M NaCl ionic strength. DPAP formulation, using PLGA 65:35 and PEI MW of ∼800 Da, demonstrated an encapsulation efficiency of 78.93%, and a loading capacity of 0.1605 mg bovine serum albumin per mg PLGA. DPAP (PLGA 65:35, PEI MW∼25 kDa) formulation showed a high release rate with a biphasic release profile. Experimental data depicted a lower targeting power and reduced drug release rate for the PEGylated DPAP formulations. The outcomes from the present study lay the foundation to optimize the performance of DPAP system as an effective synthetic drug carrier for targeted delivery.
    Matched MeSH terms: Serum Albumin, Bovine/administration & dosage; Serum Albumin, Bovine/pharmacokinetics*
  15. Preparation, characterization and in vitro release study of BSA-loaded double-walled glucose-poly(lactide-co-glycolide) microspheres
    Ansary RH, Rahman MM, Awang MB, Katas H, Hadi H, Mohamed F, et al.
    Arch Pharm Res, 2016 Sep;39(9):1242-56.
    PMID: 26818028 DOI: 10.1007/s12272-016-0710-3
    The aim of this study was to prepare a model protein, bovine serum albumin (BSA) loaded double-walled microspheres using a fast degrading glucose core, hydroxyl-terminated poly(lactide-co-glycolide) (Glu-PLGA) and a moderate-degrading carboxyl-terminated PLGA polymers to reduce the initial burst release and to eliminate the lag phase from the release profile of PLGA microspheres. The double-walled microspheres were prepared using a modified water-in-oil-in-oil-in-water (w/o/o/w) method and single-polymer microspheres were prepared using a conventional water-in-oil-in-water (w/o/w) emulsion solvent evaporation method. The particle size, morphology, encapsulation efficiency, thermal properties, in vitro drug release and structural integrity of BSA were evaluated in this study. Double-walled microspheres prepared with Glu-PLGA and PLGA polymers with a mass ratio of 1:1 were non-porous, smooth-surfaced, and spherical in shape. A significant reduction of initial burst release was achieved for the double-walled microspheres compared to single-polymer microspheres. In addition, microspheres prepared using Glu-PLGA and PLGA polymers in a mass ratio of 1:1 exhibited continuous BSA release after the small initial burst without any lag phase. It can be concluded that the double-walled microspheres made of Glu-PLGA and PLGA polymers in a mass ratio of 1:1 can be a potential delivery system for pharmaceutical proteins.
    Matched MeSH terms: Serum Albumin, Bovine/chemical synthesis*; Serum Albumin, Bovine/metabolism
  16. Attenuated Total Reflection Fourier Transform Infrared (ATR FT-IR) Spectroscopy as an Analytical Method to Investigate the Secondary Structure of a Model Protein Embedded in Solid Lipid Matrices
    Zeeshan F, Tabbassum M, Jorgensen L, Medlicott NJ
    Appl Spectrosc, 2018 Feb;72(2):268-279.
    PMID: 29022355 DOI: 10.1177/0003702817739908
    Protein drugs may encounter conformational perturbations during the formulation processing of lipid-based solid dosage forms. In aqueous protein solutions, attenuated total reflection Fourier transform infrared (ATR FT-IR) spectroscopy can investigate these conformational changes following the subtraction of spectral interference of solvent with protein amide I bands. However, in solid dosage forms, the possible spectral contribution of lipid carriers to protein amide I band may be an obstacle to determine conformational alterations. The objective of this study was to develop an ATR FT-IR spectroscopic method for the analysis of protein secondary structure embedded in solid lipid matrices. Bovine serum albumin (BSA) was chosen as a model protein, while Precirol AT05 (glycerol palmitostearate, melting point 58 ℃) was employed as the model lipid matrix. Bovine serum albumin was incorporated into lipid using physical mixing, melting and mixing, or wet granulation mixing methods. Attenuated total reflection FT-IR spectroscopy and size exclusion chromatography (SEC) were performed for the analysis of BSA secondary structure and its dissolution in aqueous media, respectively. The results showed significant interference of Precirol ATO5 with BSA amide I band which was subtracted up to 90% w/w lipid content to analyze BSA secondary structure. In addition, ATR FT-IR spectroscopy also detected thermally denatured BSA solid alone and in the presence of lipid matrix indicating its suitability for the detection of denatured protein solids in lipid matrices. Despite being in the solid state, conformational changes occurred to BSA upon incorporation into solid lipid matrices. However, the extent of these conformational alterations was found to be dependent on the mixing method employed as indicated by area overlap calculations. For instance, the melting and mixing method imparted negligible effect on BSA secondary structure, whereas the wet granulation mixing method promoted more changes. Size exclusion chromatography analysis depicted the complete dissolution of BSA in the aqueous media employed in the wet granulation method. In conclusion, an ATR FT-IR spectroscopic method was successfully developed to investigate BSA secondary structure in solid lipid matrices following the subtraction of lipid spectral interference. The ATR FT-IR spectroscopy could further be applied to investigate the secondary structure perturbations of therapeutic proteins during their formulation development.
    Matched MeSH terms: Serum Albumin, Bovine/analysis; Serum Albumin, Bovine/chemistry
  17. Interfacial partitioning behaviour of bovine serum albumin in polymer-salt aqueous two-phase system
    Chow YH, Yap YJ, Anuar MS, Tejo BA, Ariff A, Show PL, et al.
    J Chromatogr B Analyt Technol Biomed Life Sci, 2013 Sep 1;934:71-8.
    PMID: 23911538 DOI: 10.1016/j.jchromb.2013.06.034
    A relationship is proposed for the interfacial partitioning of protein in poly(ethylene glycol) (PEG)-phosphate aqueous two-phase system (ATPS). The relationship relates the natural logarithm of interfacial partition coefficient, ln G to the PEG concentration difference between the top and bottom phases, Δ[PEG], with the equation ln G=AΔ[PEG]+B. Results showed that this relationship provides good fits to the partition of bovine serum albumin (BSA) in ATPS which is comprised of phosphate and PEG of four different molecular weight 1450g/mol, 2000g/mol, 3350g/mol and 4000g/mol, with the tie-line length (TLL) in the range of 44-60% (w/w) at pH 7.0. The decrease of A values with the increase of PEG molecular weight indicates that the correlation between ln G and Δ[PEG] decreases with the increase in PEG molecular weight and the presence of protein-polymer hydrophobic interaction. When temperature was increased, a non-linear relationship of ln G inversely proportional to temperature was observed. The amount of proteins adsorbed at the interface increased proportionally with the amount of BSA loaded whereas the partition coefficient, K remained relatively constant. The relationship proposed could be applied to elucidate interfacial partitioning behaviour of other biomolecules in polymer-salt ATPS.
    Matched MeSH terms: Serum Albumin, Bovine/isolation & purification; Serum Albumin, Bovine/chemistry*
  18. Biocompatible and mucoadhesive bacterial cellulose-g-poly(acrylic acid) hydrogels for oral protein delivery
    Ahmad N, Amin MC, Mahali SM, Ismail I, Chuang VT
    Mol Pharm, 2014 Nov 3;11(11):4130-42.
    PMID: 25252107 DOI: 10.1021/mp5003015
    Stimuli-responsive bacterial cellulose-g-poly(acrylic acid) hydrogels were investigated for their potential use as an oral delivery system for proteins. These hydrogels were synthesized using electron beam irradiation without any cross-linking agents, thereby eliminating any potential toxic effects associated with cross-linkers. Bovine serum albumin (BSA), a model protein drug, was loaded into the hydrogels, and the release profile in simulated gastrointestinal fluids was investigated. Cumulative release of less than 10% in simulated gastric fluid (SGF) demonstrated the potential of these hydrogels to protect BSA from the acidic environment of the stomach. Subsequent conformational stability analyses of released BSA by SDS-PAGE, circular dichroism, and an esterase activity assay indicated that the structural integrity and bioactivity of BSA was maintained and preserved by the hydrogels. Furthermore, an increase in BSA penetration across intestinal mucosa tissue was observed in an ex vivo penetration experiment. Our fabricated hydrogels exhibited excellent cytocompatibility and showed no sign of toxicity, indicating the safety of these hydrogels for in vivo applications.
    Matched MeSH terms: Serum Albumin, Bovine/administration & dosage*; Serum Albumin, Bovine/chemistry*
  19. Comprehensive spectroscopic studies of synergism between Gadong starch based carbon dots and bovine serum albumin
    Sonthanasamy RSA, Sulaiman NMN, Tan LL, Lazim AM
    Spectrochim Acta A Mol Biomol Spectrosc, 2019 Jul 05;218:85-96.
    PMID: 30954801 DOI: 10.1016/j.saa.2019.03.108
    Carbon dots (C-dots) were used to study the binding mechanisms with serum protein, bovine serum albumin (BSA) by using two notable binding systems known as non-covalent and covalent interaction. Interaction between C-dots and BSA were estimated by Stern-Volmer equation and Double Log Regression Model (DLRM). According to the fluorescent intensity, quenching of model carrier protein by C-dots was due to dynamic quenching for non-covalent and static quenching for covalent binding. The binding site constant, KA and number of binding site, for covalent interaction is 1754.7L/mol and n≈1 (0.6922) were determined by DLRM on fluorescence quenching results. The blue shift of the fluorescence spectrum, from 450nm to 421nm (non-covalent) and 430nm (covalent) and suggested that both the microenvironment of C-dots and protein changed in relation to the protein concentration. The fluorescence intensity results show that protein structure has a significant role in Protein-C-dots interactions and type of binding influence physicochemical properties of C-dots differently. Understanding to this bio interface is important to utilize both quantum dots and biomolecules for biomedical field. It can be a useful guideline to design further applications in biomedical and bioimaging.
    Matched MeSH terms: Serum Albumin, Bovine/metabolism*; Serum Albumin, Bovine/chemistry
  20. Rapid Surface Modification of Ultrafiltration Membranes for Enhanced Antifouling Properties
    Said N, Khoo YS, Lau WJ, Gürsoy M, Karaman M, Ting TM, et al.
    Membranes (Basel), 2020 Dec 07;10(12).
    PMID: 33297433 DOI: 10.3390/membranes10120401
    In this work, several ultrafiltration (UF) membranes with enhanced antifouling properties were fabricated using a rapid and green surface modification method that was based on the plasma-enhanced chemical vapor deposition (PECVD). Two types of hydrophilic monomers-acrylic acid (AA) and 2-hydroxyethyl methacrylate (HEMA) were, respectively, deposited on the surface of a commercial UF membrane and the effects of plasma deposition time (i.e., 15 s, 30 s, 60 s, and 90 s) on the surface properties of the membrane were investigated. The modified membranes were then subjected to filtration using 2000 mg/L pepsin and bovine serum albumin (BSA) solutions as feed. Microscopic and spectroscopic analyses confirmed the successful deposition of AA and HEMA on the membrane surface and the decrease in water contact angle with increasing plasma deposition time strongly indicated the increase in surface hydrophilicity due to the considerable enrichment of the hydrophilic segment of AA and HEMA on the membrane surface. However, a prolonged plasma deposition time (>15 s) should be avoided as it led to the formation of a thicker coating layer that significantly reduced the membrane pure water flux with no significant change in the solute rejection rate. Upon 15-s plasma deposition, the AA-modified membrane recorded the pepsin and BSA rejections of 83.9% and 97.5%, respectively, while the HEMA-modified membrane rejected at least 98.5% for both pepsin and BSA. Compared to the control membrane, the AA-modified and HEMA-modified membranes also showed a lower degree of flux decline and better flux recovery rate (>90%), suggesting that the membrane antifouling properties were improved and most of the fouling was reversible and could be removed via simple water cleaning process. We demonstrated in this work that the PECVD technique is a promising surface modification method that could be employed to rapidly improve membrane surface hydrophilicity (15 s) for the enhanced protein purification process without using any organic solvent during the plasma modification process.
    Matched MeSH terms: Serum Albumin, Bovine
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