Effect of bovine serum albumin on the functionality and structure of catanionic surfactant at air–buffer interface

Maiti, Kajari; Bhattacharya, Subhash C.; Moulik, Satya P.; Panda, Amiya Kumar

doi:10.1016/j.msec.2012.11.009

Cited by 13 publications

(5 citation statements)

References 63 publications

(59 reference statements)

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“…Similar behavior was reported earlier for bovine serum albumin and dipalmitoylphosphatidylcholine (DPPC) as well as for catanionic surfactants in the presence of BSA, proving the significant association between both compounds. 49 The hydrophobic interactions were indicated as being responsible for that phenomenon.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Physicochemical Characterization of Oleanolic Acid–Human Serum Albumin Complexes for Pharmaceutical and Biosensing Applications

2020

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Among numerous compounds found in marine organisms, triterpenes have attracted considerable research interest due to a beneficial impact on health including anti-inflammatory, antitumor, antiviral, and antioxidation effects. Specifically, new functionalities of oleanolic acid (OLA) have been revealed recently, indicating possible applications in nutrition and pharmaceuticals. However, this bioactive material has limited value due to low water solubility and stability. Therefore, oleanolic acid needs a carrier that protects it and enables controlled release in the human body. Innovative drug delivery systems provide a promising strategy for overcoming these problems. However, the development of those systems requires a comprehensive understanding of the physicochemical properties of triterpenes and their carriers as well as the interactions between them. Among numerous substances, human serum albumin (HSA) has been widely studied as a drug carrier. In addition, human serum albumin is the main blood plasma protein responsible for the transport of drugs and metabolites; therefore, the interactions between that protein and other substances are of physiological and pharmaceutical importance. Moreover, sensing the HSA level in blood plasma is an important challenge that requires binding studies on a molecular scale. The aim of this study was to investigate the properties of oleanolic acid in the presence of human serum albumin in terms of thermodynamics, morphology, and viscoelasticity at the air/water interface. Moreover, the wettability, surface free energy, and topography of the films after deposition on the solid substrate were determined. The results have been discussed in terms of providing physicochemical insight into the interfacial behavior of the OLA–HSA complex, which is crucial for pharmaceutical and bioanalytical applications.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Physicochemical Characterization of Oleanolic Acid–Human Serum Albumin Complexes for Pharmaceutical and Biosensing Applications

2020

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“…And the first-order rate constant ( κ ) was calculated to learn the desorption process of BSA. It can be obtained from the equation ( 2 ) 34 . where π t , π i and π f are the surface pressure of monolayer at time t , initial and final, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…K. Maiti et al . 34 have proposed that the desorption rate of BSA was decreased with the increasing of [BSA], which was because the inter-protein molecular interaction slowed down the desorption rate. The order of κ values of mixed DOTAP-BSA monolayer was κ pH=3 < κ pH=10 < κ pH=5 .…”

Section: Resultsmentioning

confidence: 99%

The interaction between BSA and DOTAP at the air-buffer interface

Hao

Zhang

et al. 2018

Sci Rep

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In this article, the interaction between bovine serum albumin (BSA) and the cationic 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP) at the air-buffer interface was investigated at different subphase’s pH values (pH = 3, 5 and 10). Surface pressure measurements (π − A) and penetration kinetics process (π − t) were carried out to reveal the interaction mechanism and the dynamical behavior. The data showed that π − A isotherms moved towards larger mean molecular area when the concentration of BSA ([BSA]) increased, the amount of BSA adsorbed onto DOTAP monolayer reached a threshold value at a [BSA] of 5 × 10−8 M, and BSA desorbed from the lipid monolayer as time goes by. The results revealed that the association of BSA with DOTAP at the air-buffer interface was affected by the subphase’s pH value. When pH = 10, the interaction mechanism between them was a combination of hydrophobic interaction and electrostatic attraction, so BSA molecules could be well separated and purified from complex mixtures. AFM images demonstrated that pH value and [BSA] could affect the morphology feature of DOTAP monolayer and the adsorption and desorption processes of BSA. So the study provides an important experimental basis and theoretical support for learning the interaction mechanism among biomolecules in separation and purification of biomolecules and biosensor.

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“…Another process influencing radius of gyration occurs when more and more surfactant molecules bind to the protein. The negative net charge of BSA diminishes upon attaching many positive gemini molecules, and then the protein lacks solubility [ 48 ]. This effect is clearly visible in examined solutions.…”

Section: Resultsmentioning

confidence: 99%

“…In both prepared SAXS and CD samples, BSA could be neutralised around the molar ratio of gemini-to-BSA of 8.3:1, rather than e.g. 17:1, as the charge of gemini surfactants is equal to 2, and BSA net charge at pH of 7 is −17 [ 48 ]. As pointed above, reduction of protein net charge results in molecules attraction, and at c surf : c BSA = 8.3, a significant growth of BSA R g was observed.…”

Section: Resultsmentioning

confidence: 99%

Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL

Gospodarczyk

Kozak

2015

Colloid Polym Sci

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Gemini surfactants and their interactions with proteins have gained considerable scientific interest, especially when amyloidogenic proteins are taken into account. In this work, the influence of two selected dicationic (gemini) surfactants (3,3′-[1,8-(2,7-dioxaoctane)]bis(1-dodecylimidazolium) chloride and 3,3′-[1,12-(2,11-dioxadodecane)]bis(1-dodecylimidazolium) chloride) on two model proteins, bovine serum albumin (BSA) and hen egg white lysozyme (HEWL), have been investigated. A pronounced and sophisticated influence on BSA structure has been revealed, including a considerable change of protein radius of gyration as well as substantial alteration of its secondary structure. Radius of gyration has been found to rise significantly with addition of surfactants and to fall down for high surfactants concentration. Similarly, a remarkable fall of secondary structure (α-helix content) has been observed, followed by its partial retrieval for high surfactants concentration. A strong aggregation of BSA has been observed for a confined range of surfactants concentrations as well. In case of HEWL-gemini system, on the other hand, the protein-surfactant interaction was found to be weak. Molecular mechanisms explaining such behaviour of protein-surfactant systems have been proposed. The differences of properties of both studied surfactants have also been discussed.

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Effect of bovine serum albumin on the functionality and structure of catanionic surfactant at air–buffer interface

Cited by 13 publications

References 63 publications

Physicochemical Characterization of Oleanolic Acid–Human Serum Albumin Complexes for Pharmaceutical and Biosensing Applications

Physicochemical Characterization of Oleanolic Acid–Human Serum Albumin Complexes for Pharmaceutical and Biosensing Applications

The interaction between BSA and DOTAP at the air-buffer interface

Interaction of two imidazolium gemini surfactants with two model proteins BSA and HEWL

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