Investigation of bovine serum albumin-surfactant aggregation and its physicochemical characteristics

Misra, Pratibha; Das, B.; Maharana, Suprava

doi:10.1016/j.colsurfa.2015.06.052

Cited by 37 publications

(29 citation statements)

References 48 publications

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“…The authors concluded that fluorescence intensity decreases significantly with the increase of the cationic gemini surfactant concentration. A similar trend has been reported in single-chain surfactant-BSA interactions, such as cationic DTAB-BSA [34] and TTAB-BSA [18].…”

Section: Fluorescence Measurementssupporting

confidence: 83%

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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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Section: Fluorescence Measurementssupporting

confidence: 83%

“…The authors suggested that hydrophobic and electrostatic forces play an important role in protein-surfactant interactions. Dodecyl trimethylammonium bromide (DTAB), tetradecyltrimethylammonium bromide (TTAB) and CTAB have been reported to act as chemical chaperones, aiding in the refolding of proteins via hydrophobic interactions [18].…”

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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“…This leads to the separation of RMP from the other biomolecules in MDF. Within the water pool, RMP arranges itself to get minimal free‐energy constraints [39, 40, 43]. Consequently, the driving forces for the solubilisation of RMP within the water pool are: (i) the electrostatic attraction between the hydrophilic surfactant (headgroups) of AOT and charged regions of the protein; and (ii) the hydrophobic interactions among the nonpolar segments of the protein.…”

Section: Resultsmentioning

confidence: 99%

“…On the other hand, the protein can assume charged or neutral character depending on the pH of its immediate environment and its isoelectric point. For most of the proteins, the isoelectric point lies within 4.8–5.0 [39, 40]. To ascertain the solubilisation site and nature of orientation of the protein present in MDF within an RM, the point of zero charge (PZC) and natural pH of MDF in water were determined (Fig.…”

Section: Resultsmentioning

confidence: 99%

Isolation, process optimisation and characterisation of the protein from the de‐oiled cake flour of Madhuca latifolia

Biswal

Panda

Yang

et al. 2020

IET nanobiotechnol.

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“…The results of interaction between BSA and DHDAB, THDAB, CHDAB are similar to the interaction between BSA and traditional quaternary ammonium cationic surfactants: dodecyltrimethylammonium bromide (DTAB), tetradecyltrimethylammonium bromide (TTAB), and cetyltrimethylammonium bromide (CTAB). While, since the existence of -OH group, the electrostatic interaction between DHDAB, THDAB, CHDAB and BSA is stronger than the electrostatic interaction between DTAB, TTAB, CTAB and BSA 51 .…”

Section: Discussionmentioning

confidence: 97%

The Interactions between Quaternary Ammonium Cationic Surfactants and Bovine Serum Albumin

浙江工商大学应用化学系¹,

Liu²,

Sun³

et al. 2016

Acta Physico-Chimica Sinica

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UV-visible (UV-Vis) absorption spectroscopy, fluorescence spectroscopy (FL), dynamic light scattering (DLS) and isothermal titration calorimetry (ITC) were used to study the interactions between bovine serum albumin (BSA) and the three quaternary ammonium surfactants N-dodecyl-N-(2-hydroxyethyl)-N,Ndimethyl ammonium bromide (DHDAB), N-tetradecyl-N-(2-hydroxyethyl)-N,N-dimethyl ammonium bromide (THDAB) and N-cetyl-N-(2-hydroxyethyl)-N,N-dimethyl ammonium bromide (CHDAB). These surfactants quenched the intrinsic fluorescence of BSA, with longer alkyl chains resulting in more significant quenching. This was attributed to static quenching. Further evidence of static quenching was provided by UV-Vis absorption spectroscopy. The particle size of BSA was found to initially increase and then decrease with increasing surfactant concentration. The concentration of surfactant changed the type of interaction mode. This work revealed the mechanism and binding characteristics between surfactants and protein, and provides the basis

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Investigation of bovine serum albumin-surfactant aggregation and its physicochemical characteristics

Cited by 37 publications

References 48 publications

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

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

Isolation, process optimisation and characterisation of the protein from the de‐oiled cake flour of Madhuca latifolia

The Interactions between Quaternary Ammonium Cationic Surfactants and Bovine Serum Albumin

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