Binding interaction of an anionic amino acid surfactant with bovine serum albumin: physicochemical and spectroscopic investigations combined with molecular docking study

Dasmandal, Somnath; Kundu, Arjama; Rudra, Suparna; Mahapatra, Ambikesh

doi:10.1039/c5ra17254c

Cited by 39 publications

(15 citation statements)

References 70 publications

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“…Dasmandal et al . 9 used molecular docking and spectroscopy experiments and found that the binding of anionic amino acid surfactant (AAS) to BSA occurred between hydrophobic subdomain IIA and IIIA where tryptophan-213 residue is located. They observed multiple hydrogen bonding and hydrophobic interactions between the AAS ligand and the BSA which agrees with the current study.…”

Section: Discussionmentioning

confidence: 99%

“…Bovine Serum Albumin (BSA) is an abundant plasma protein and a universal bio-reagent used in numerous applications, such as enzyme linked immunosorbent assays and immunofluorescence microscopy 2,4,9 . The crystal structure of BSA consists of three homologous domains, each in turn is divided into sub-domain A and B 6 .…”

Section: Introductionmentioning

confidence: 99%

“…When surfactants interact with the BSA protein, they modify the structure of the protein which affects the interactions of the protein with pharmaceutical substances (e.g. drugs) 9 . The encapsulation of these pharmaceutical substances in surfactants or polymer/surfactant mixtures modulates their release.…”

Section: Introductionmentioning

confidence: 99%

“…The interactions of BSA with surfactants have been studied by various experimental techniques in attempt to gain an in-depth knowledge of the structural modifications occurring at each binding stage 1 . Some of the experimental methods used include microscopy 7 , spectroscopy 2,8,9 and small angle scattering 1 . Though the binding strengths of various categories of surfactants with BSA have been identified 4,8 , the balance of the driving force is unclear.…”

Section: Introductionmentioning

confidence: 99%

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In Silico Characterization of the Binding Modes of Surfactants with Bovine Serum Albumin

Nnyigide

Lee

Hyun

2019

Sci Rep

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The binding interactions of the surfactants: anionic sodium dodecyl sulphate (SDS), cationic cetyltrimethylammonium bromide (CTAB), non-ionic octyl glucoside (OG), and zwitterionic 3-[Hexadecyl(dimethyl)ammonio]-1-propanesulfonate (HPS), with bovine serum albumin (BSA) were investigated by computer simulation. The results disclosed that the surfactants bound stably between hydrophobic subdomain IIA and IIIA where tryptophan-213 residue, an important intrinsic fluorophore in BSA is housed. The interactions of the surfactants with the BSA were electrostatic and hydrophobic interactions. The head-groups of SDS, HPS and OG formed hydrogen bonds with the BSA, while that of CTAB was shielded from intermolecular hydrogen-bonding due to intervening methyl groups. Subsequently, molecular dynamics (MD) simulation of the protein-surfactant complexes revealed that hydrogen bonds formed by OG were stronger than those of SDS and HPS. However, the decomposed force-field energies showed that OG had the least interaction energy with the BSA. In addition to MD simulation, it was found by density functional theory (DFT) that the differences in the coulomb interaction energies can be attributed to charge distribution in the surfactants. Overall, free energies calculated by linear interaction energy (LIE) proved that the binding of each surfactant was dominated by differences between van der Waals interactions in bound and free states.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

In Silico Characterization of the Binding Modes of Surfactants with Bovine Serum Albumin

Nnyigide

Lee

Hyun

2019

Sci Rep

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“…Among the serum albumins, BSA has been widely used in biophysical studies to clarifying the binding mechanism of small molecules to proteins due to its physiological functions and 76% of structural similarity with Human Serum Albumin (HSA) (Sułkowska, 2002;Dasmandal et al, 2015). Investigation on binding of drugs to serum albumins may help us to understand drug's distribution and toxicity in the biological systems.…”

Section: Introductionmentioning

confidence: 99%

Binding Mechanism of Bovine Serum Albumin to Troxerutin by Synchronous Fluorescence Spectroscopy and Chemometrics

Wang¹,

Yan²,

Luo³

2016

American Journal of Biochemistry and Biotechnology

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Previous works have reported the binding of Bovine Serum Albumin (BSA) to troxerutin by absorption and fluorescence spectroscopy. In order to extend the investigation of their binding characteristics, the study presented here was designed to evaluate their interaction by the synchronous fluorescence spectroscopy and Multivariate Curve Resolution With Alternating Least Squares (MCR-ALS) under simulative physiological conditions. The Evolving Factor Analysis (EFA) and MCR-ALS analysis results show that there are three chemical species in the troxerutin-BSA system, which reveal that the fluorescence quenching of BSA caused by troxerutin may be a static quenching mechanism. The spectral profile of each compound was obtained by the soft of MCR-ALS. The obtained average binding constant is 6.43×10 5 mol −1 L for BSA and troxerutin concentration ratio is 7 while that is 6.89×10 5 mol −1 L for troxerutin and BSA concentration ratio is 5. The study might further help us to better understand the structural features and toxicological action of troxerutin at the molecular level.

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Insights into the binding interaction between copper ferrite nanoparticles and bovine serum albumin: An effect on protein conformation and activity

et al. 2018

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The binding affinity between bovine serum albumin (BSA) and copper ferrite (CuFe O ) nanoparticles in terms of conformation, stability and activity of protein was studied using various spectroscopic methods. The quenching involved in BSA-CuFe O NP interaction was static quenching as analysed by different techniques (steady-state and time-resolved fluorescence along with temperature-dependent fluorescence measurements). Among all types of possible interactions, it was revealed that the major binding forces were van der Waals interaction and hydrogen bonding, which were explored from negative values of enthalpy change (∆H = -193.85 kJ mol ) and entropy change (∆S = -588.88 J mol K ). Additionally, synchronous, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy measurements confirmed the conformational changes in BSA upon the addition of CuFe O NP. Furthermore, thermal denaturation observations were consistent with the circular dichroism results. The interaction of CuFe O NP with BSA decreased the esterase activity in the BSA assay, revealing the affinity of copper ferrite towards the active site of BSA.

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Binding interaction of an anionic amino acid surfactant with bovine serum albumin: physicochemical and spectroscopic investigations combined with molecular docking study

Abstract: Exploration of binding interaction between anionic amino acid surfactant and BSA.

Cited by 39 publications

References 70 publications

In Silico Characterization of the Binding Modes of Surfactants with Bovine Serum Albumin

In Silico Characterization of the Binding Modes of Surfactants with Bovine Serum Albumin

Binding Mechanism of Bovine Serum Albumin to Troxerutin by Synchronous Fluorescence Spectroscopy and Chemometrics

Insights into the binding interaction between copper ferrite nanoparticles and bovine serum albumin: An effect on protein conformation and activity

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