Interaction of bovine serum albumin with cationic monomeric and dimeric surfactants: A comparative study

Kumar, Birendra; Lakra, Jyotsna; Yadav, Toshikee; Kumari, Suman; Saha, Sarani; Ghosh, Kallol K.

doi:10.1016/j.molliq.2016.02.052

Cited by 37 publications

(26 citation statements)

References 38 publications

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“…[34][35][36] The quenching mechanism can be classified as dynamic quenching (collisional system) or static quenching (complex formation) between fluorophores and quenchers. 37 Dynamic and static quenching can be distinguished by their different relations on temperature and viscosity. 38 The probability of fluorescence quenching with ligands depends on the rate of collision of the quencher and the ground-state fluorophore (static quenching) or excited fluorophore (dynamic quenching).…”

Section: Thermodynamic Parametersmentioning

confidence: 99%

Albumin binding, anticancer and antibacterial properties of synthesized zero valent iron nanoparticles

Anbouhi¹,

Esfidvajani²,

Nemati³

et al. 2018

IJN

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BackgroundNanoparticles (NPs) have been emerging as potential players in modern medicine with clinical applications ranging from therapeutic purposes to antimicrobial agents. However, before applications in medical agents, some in vitro studies should be done to explore their biological responses.AimIn this study, protein binding, anticancer and antibacterial activates of zero valent iron (ZVFe) were explored.Materials and methodsZVFe nanoparticles were synthesized and fully characterized by X-ray diffraction, field-emission scanning electron microscope, and dynamic light scattering analyses. Afterward, the interaction of ZVFe NPs with human serum albumin (HSA) was examined using a range of techniques including intrinsic fluorescence, circular dichroism, and UV–visible spectroscopic methods. Molecular docking study was run to determine the kind of interaction between ZVFe NPs and HSA. The anticancer influence of ZVFe NPs on SH-SY5Y was examined by MTT and flow cytometry analysis, whereas human white blood cells were used as the control cell. Also, the antibacterial effect of ZVFe NPs was examined on Pseudomonas aeruginosa (ATCC 27853), Escherichia coli (ATCC 25922), and Staphylococcus aureus (ATCC 25923).ResultsX-ray diffraction, transmission electron microscope, and dynamic light scattering analyses verified the synthesis of ZVFe NPs in a nanosized diameter. Fluorescence spectroscopy analysis showed that ZVFe NPs spontaneously formed a complex with HSA through hydrogen bonds and van der Waals interactions. Also, circular dichroism spectroscopy study revealed that ZVFe NPs did not change the secondary structure of HSA. Moreover, UV–visible data presented that melting temperature (Tm) of HSA in the absence and presence of ZVFe NPs was almost identical. Molecular dynamic study also showed that ZVFe NP came into contact with polar residues on the surface of HSA molecule. Cellular assays showed that ZVFe NPs can induce cell mortality in a dose-dependent manner against SH-SY5Y cells, whereas these NPs did not trigger significant cell mortality against normal white bloods in the concentration range studied (1–100 µg/mL). Antibacterial assays showed a noteworthy inhibition on both bacterial strains.ConclusionIn conclusion, it was revealed that ZVFe NPs did not induce a substantial influence on the structure of protein and cytotoxicity against normal cell, whereas they derived significant anticancer and antibacterial effects.

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Section: Thermodynamic Parametersmentioning

confidence: 99%

Albumin binding, anticancer and antibacterial properties of synthesized zero valent iron nanoparticles

Anbouhi¹,

Esfidvajani²,

Nemati³

et al. 2018

IJN

View full text Add to dashboard Cite

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“…mouthwash products and oral antiseptics). Their adverse effects can be avoided by the use of soft analogues of long-chain QACs, which are synthesized according to the soft drug approach and their physicochemi-as human serum albumin (HSA) [12] and bovine serum albumin (BSA) [13,14] can contribute towards a better understanding of the action of surfactants as solubilizing agents of membranes containing proteins and lipids [15]. BSA is commonly used as an expedient protein and is widely implicated as a general model to study the interactions of surfactants [14] and drugs [16] with globular proteins, not only due to its important roles in biological processes, but also because its structure is well established.…”

Section: Introductionmentioning

confidence: 99%

Physicochemical study of biomolecular interactions between lysosomotropic surfactants and bovine serum albumin

Janek

Czyżnikowska

Łuczyński

et al. 2017

Colloids and Surfaces B: Biointerfaces

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The interactions between two cationic lysosomotropic surfactants (2-dodecanoyloxyethyl)trimethylammonium bromide (DMM-11) and (2-dodecanoyloxypropyl)trimethylammonium bromide (DMPM-11) with bovine serum albumin (BSA) in Hepes buffer (pH=7.4) were systematically studied by surface tension, fluorescence and circular dichroism (CD) spectroscopy and isothermal titration calorimetry (ITC). Furthermore, the size of the micellar aggregates and the polydispersity indexes of both cationic surfactants were studied by dynamic light scattering technique (DLS). The hydrodynamic radii, micellar volumes and aggregation numbers were calculated using a method based on density functional theory (DFT). The results showed that, in both cases, the surface tension was modified upon addition of BSA, and the critical micelle concentration (CMC) values of DMM-11 and DMPM-11 were higher in the presence of BSA. The fluorescence intensity of BSA decreased significantly as the concentration of both cationic surfactants increased and this effect was attributed to the formation of surfactant-BSA complexes. Synchronous fluorescence spectrometry showed the binding-induced conformational changes in BSA. Finally, CD and DLS results revealed the occurrence of changes in the secondary structure of the protein in the presence of both surfactants. In conclusion, understanding the interactions between lysosomotropic surfactants and BSA is required to explore their potential applications in medicine.

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“…In the main Figures and it can be seen that, at pH 7.4 and 11, respectively, the addition of 0.1 M SDS quenched the fluorescence emission of 1 × 10 −5 M BSA with a blue shift near to ~10 nm with respect to the aqueous buffer solution. This phenomenon has been extensively studied and reported by other authors for SDS as well for other surfactants and was attributed to the exposure of the Trp residues of BSA to the environment given by the surfactant. Low surfactant concentrations induce changes in Trp 214 vicinity while at high concentrations the changes around Trp 135 are responsible for the quenching by SDS.…”

Section: Resultsmentioning

confidence: 63%

Influence of pH and micellar systems on the sensitized photo‐oxidation of bovine serum albumin

et al. 2019

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Photosensitized oxidation of bovine serum albumin (BSA), by using perinaphtenone as a sensitizer, has been studied at pH 7.4 and 11. The selected sensitizer does not present ground‐state complexation with BSA and ensures that the mechanism is mediated by O2(1△g). Strong dependence between BSA–O2(1△g) photo‐oxidation and the pH of the medium has been found. The relative oxygen uptake rate (v− △ O2) and the total quenching rate constant (kt) values are higher at pH 11 than pH 7.4. The enhancement in the alkaline condition is due to conformational changes in the protein and the reactivity of tyrosinate anion with O2(1△g). Even when the tendency with the pH in the presence of sodium dodecyl sulfate (SDS) micelles is similar to that observed in homogeneous media, an increment on the kt value is detected. This effect may be attributable to the strong interaction of BSA–SDS, which leads to the protein unfolding and could leave more exposed photo‐oxidizable amino acids. A protective effect against the O2(1△g)‐mediated photo‐oxidation was observed in reverse micelles (RMs) of sodium bis(2‐ethylhexyl)sulfosuccinate (AOT) by comparing the kt values obtained at W = 10 with respect to the one obtain in homogeneous media. The latter could be mainly explained by the modification in the solvent polarity. Also, another important observation was found, the internal pH inside RMs of AOT sensed through tyrosine absorption was independent of the one used for the formation of the water pool. Hence, the kt values observed at both pH, are quite similar.

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Interaction of bovine serum albumin with cationic monomeric and dimeric surfactants: A comparative study

Cited by 37 publications

References 38 publications

Albumin binding, anticancer and antibacterial properties of synthesized zero valent iron nanoparticles

Albumin binding, anticancer and antibacterial properties of synthesized zero valent iron nanoparticles

Physicochemical study of biomolecular interactions between lysosomotropic surfactants and bovine serum albumin

Influence of pH and micellar systems on the sensitized photo‐oxidation of bovine serum albumin

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