scholarly journals Nanocoatings of Bovine Serum Albumin on Glass: Effects of pH and Temperature

2020 ◽  
Vol 2020 ◽  
pp. 1-11
Author(s):  
Sergio-Miguel Acuña-Nelson ◽  
José-Miguel Bastías-Montes ◽  
Fabiola-Rossana Cerda-Leal ◽  
Julio-Enrique Parra-Flores ◽  
Juan-Salvador Aguirre-García ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Self Assembly ◽  
Glass Surface ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Dynamic Contact ◽  
Dlvo Theory ◽  
Contact Angles ◽  
Protein Size

Protein adsorption is influenced by many factors such as temperature, pH, protein size and structure, or surface energy and roughness, among others. Self-assembled monolayers (SAMs) and the Langmuir-Blodgett (LB) technique are two of the techniques more used to produces ultrathin films of proteins on surfaces. In this work, we established protocols for the preparation of nanocoatings of bovine serum albumin (BSA) protein on glass surface using SAMs and LB. Furthermore, we determined how small changes in temperature and pH can affect the covering when SAMs are used. Using a combination of different analyses, such as relative roughness, dynamic contact angles, and atomic force microscopy (AFM), it was possible to establish conditions to obtain a uniform nanocoating using SAMs. The results of the analysis of the nanocoating performed using the LB technique were very similar to those obtained using SAMs. The Derjaguin–Landau–Verwey–Overbeek (DLVO) theory in conjunction with the AFM images showed that electrostatic interactions are very important in the self-assembly process, but a process dominated solely by attraction is not sufficient to achieve a good SAM nanocoating, since it does not allow proper orientation and packaging of BSA molecules on the glass surface.

scholarly journals Physicochemical Peculiarities of Iodine-Dimethylsulfoxide-H2O Solutions and Effect on Ion Binding to Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-5
Author(s):  
K. Grigoryan ◽  
H. Shilajyan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Ion Binding ◽  
Fluorescence Energy Transfer ◽  
Iodide Ion ◽  
Different Temperatures ◽  
Fluorescence Energy

The interaction of iodine with bovine serum albumin (BSA) in dimethylsulfoxide (DMSO) aqueous solutions was studied by means of fluorescence and UV/Vis absorption spectroscopy methods. Physicochemical peculiarities of these solutions were revealed. The results showed that the tri-iodide ion formed in the 1DMSO : 2H2O solution caused the fluorescence quenching of BSA. The modified Stern-Volmer quenching constant and corresponding thermodynamic parameters, the free energy change (), enthalpy change (), and entropy change (), at different temperatures (293, 298, and 303 K) were calculated, which indicated that the hydrophobic and electrostatic interactions were the predominant operating forces. The binding locality distance r between BSA and tri-iodide ion at different temperatures was determined based on Förster nonradiation fluorescence energy transfer theory.

Modulations in the self-assembly of bovine serum albumin by enhanced depolymerisation and condensation induced upon stirring

RSC Advances ◽  
2016 ◽  
Vol 6 (95) ◽  
pp. 92349-92359
Author(s):  
Shivnetra Saha ◽  
Rupali Shekhawat ◽  
Shashank Deep
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Self Assembly ◽  
Bovine Serum ◽  
The Self ◽  
Unusual Phenomenon

An unusual phenomenon in the aggregation profile of BSA in the presence of CTAB, brought about by stirring, is reported here.

scholarly journals Self-assembled bovine serum albumin nanoparticles as pesticide delivery vectors for controlling trunk-boring pests

2020 ◽  
Vol 18 (1) ◽  
Author(s):  
Chenyu Su ◽  
Shanshan Liu ◽  
Shenghan Cao ◽  
Shuyan Yin ◽  
Chenggang Zhou ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Self Assembly ◽  
Bovine Serum ◽  
Fluorescein Isothiocyanate ◽  
Effective Control ◽  
Transport Efficiency ◽  
Dead Trees ◽  
Self Assembled ◽  
And Control

Abstract Background Trunk-boring pests (TBPs) are an important type of forest pest, TBPs not only feed on the branches and trunks of trees, but also spread quarantine diseases in forests. However, because the larvae of TBPs live inside the trunk and are well concealed, prevention and control are difficult. The lack of effective control methods leads to the death of many trees in forests. In this study, a novel nanopesticide featuring high bioactivity and slow-release properties was developed to control TBPs. Thiacloprid (THI), which is commonly used to control Coleoptera species, was used as a model pesticide. Results The oleophobic properties of bovine serum albumin (BSA) were exploited to encapsulate the hydrophobic pesticide THI by self-assembly, and the size of the obtained nanoparticles, THI@BSA·NPs, was approximately 23 nm. The loading efficiency reached 70.4%, and THI@BSA·NPs could be released continuously for over 15 days, with the cumulative release reaching 93.5%. The fluorescein isothiocyanate (FITC)-labeled nanoparticles were evenly distributed in the digestive tract and body surface of a typical TBPs, M. alternatus, and the stomach and contact toxicities increased by 33.7% and 25.9%, respectively, compared with those of free THI. Furthermore, the results showed that the transport efficiency of THI@BSA·NPs was highest at a concentration of 50 μg/mL, and the THI@BSA·NPs content in the trunk, from to lower to higher layers, was 8.8, 8.2, 7.6, and 5.8 μg/g. At the same time, THI@BSA·NPs also exhibited high transport efficiency in dead trees. Conclusion The transport efficiency and toxicity of the active ingredients are the key factors for the control of TBPs. This work provided idea for the application of biological delivery system encapsulated hydrophobic pesticides. The novel self-assembled THI@BSA·NPs have promising potential for sustainable control of TBPs.

Contribution of Surface Charge to Bovine Serum Albumin Adsorption on Hydroxyapatite Ceramic Particles

2007 ◽  
Vol 330-332 ◽  
pp. 861-864 ◽  
Author(s):  
Xiang Dong Zhu ◽  
Hong Song Fan ◽  
X. N. Chen ◽  
Dong Xiao Li ◽  
Xing Dong Zhang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Charge ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Solid Particles ◽  
Hydroxyapatite Ceramic ◽  
Liquid Environment ◽  
Zeta Potentials ◽  
Albumin Adsorption

Protein adsorption is driven by various interactions. The contribution of surface charge to bovine serum albumin (BSA) adsorption on hydroxyapatite (HA) ceramic was investigated by adjusting the liquid environment in which the solid particles dispersed. Zeta potentials of HA and the adsorption of BSA on the surface were tested as a function of pH, ionic strength, Ca2+ and PO4 3- concentrations in the aqueous solutions, and the results showed that both of them were greatly affected by those experimental variations. Besides, the amount of adsorbed BSA was related to the variation of zeta potential of HA, as could be well understood in terms of electrostatic interactions.

scholarly journals Complex coacervates between bovine serum albumin and anionic polysaccharides: formation and characterization

2021 ◽  
Vol 24 ◽  
Author(s):  
Lorena Oliveira Ferreira ◽  
Monique Barreto Santos ◽  
Edwin Elard Garcia-Rojas
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Initial Study ◽  
Wide Ph Range ◽  
The Fourier Transform ◽  
Ph Range ◽  
The Comparative Study ◽  
Maximum Turbidity

Abstract The comparative study regarding complexes coacervated between Bovine Serum Albumin (BSA) and different polysaccharides, Pectin (PEC) and Gum Acacia (GA), was carried out by evaluating the influence of different ratios (protein:polysaccharide) and sodium chloride (NaCl) concentrations on turbidity and zeta potential. The BSA:PEC complexes were formed in a 10:1 ratio whereas BSA:GA at 3:1. The complexation pH showed different behavior, BSA: PEC complexes exhibited maximum turbidity in a wide pH range (4.9 to 1.5), while BSA: GA had maximum turbidity at pH 3.5. The increase in the concentration of NaCl negatively influenced the complexation. The NaCl concentration of 0.40 mol L-1 suppressed the interaction in BSA:PEC (10:1) and reduced the range formation of BSA:GA (3:1). The Fourier Transform Infrared (FTIR) demonstrated the participation not only of electrostatic interactions, but also of hydrogen bonds in the complexation. This initial study elucidated fundamental aspects about the formation of coacervate complexes between BSA:GA/PEC that assist in directing its application in food products especially, in acidic matrices (pH~4.0) as well as with low concentration of salts, in view of the effect of pH on maximum formation and sensitivity to NaCl. These complexes can be added directly to products in order to add nutritional value or even be used as a new matrix for the encapsulation of bioactive compounds.

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