Interaction of biocompatible natural rosin-based surfactants with human serum albumin: A biophysical study

Ishtikhar, Mohd; Ali, Mushir; Atta, Ayman M.; Al‐Lohedan, Hamad A.; Nigam, Lokesh; Subbarao, Naidu; Khan, Rizwan Hasan

doi:10.1016/j.jlumin.2015.06.012

Cited by 28 publications

(7 citation statements)

References 56 publications

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“…The reactions are consistent with the “enthalpy–entropy compensation effect”, in which the enthalpy drop due to the deformation of hydrogen bonds is counter-balanced by the entropic penalty due to the burial of involved groups in the interaction 30 . This effect is frequently found in other ligand–protein interactions 31 , 32 . The free energy (Δ G ) was calculated from Eq.…”

Section: Resultsmentioning

confidence: 63%

Binding modes of environmental endocrine disruptors to human serum albumin: insights from STD-NMR, ITC, spectroscopic and molecular docking studies

Yang

Huang

Liu

et al. 2017

Sci Rep

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Given that bisphenols have an endocrine-disrupting effect on human bodies, thoroughly exposing their potential effects at the molecular level is important. Saturation transfer difference (STD) NMR-based binding studies were performed to investigate the binding potential of two bisphenol representatives, namely, bisphenol B (BPB) and bisphenol E (BPE), toward human serum albumin (HSA). The relative STD (%) suggested that BPB and BPE show similar binding modes and orientations, in which the phenolic rings were spatially close to HSA binding site. ITC analysis results showed that BPB and BPE were bound to HSA with moderately strong binding affinity through electrostatic interactions and hydrogen bonds. The order of binding affinity of HSA for two test bisphenols is as follows: BPE > BPB. The results of fluorescence competitive experiments using 5-dimethylaminonaphthalene-1-sulfonamide and dansylsarcosine as competitors, combined with molecular docking indicated that both bisphenols are prone to attach to the binding site II in HSA. Spectroscopic results (FT-IR, CD, synchronous and 3D fluorescence spectra) showed that BPB/BPE induces different degrees of microenvironmental and conformational changes to HSA.

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Section: Resultsmentioning

confidence: 63%

Binding modes of environmental endocrine disruptors to human serum albumin: insights from STD-NMR, ITC, spectroscopic and molecular docking studies

Yang

Huang

Liu

et al. 2017

Sci Rep

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“…Under fixed pH conditions, temperature and ionic strength, fluorescence quenching may ensue from ground‐state complex formation, energy transfer and dynamic quenching processes. Dynamic quenching refers to a process in which the fluorophore and the quencher ([Cu(carmoisine) 2 (H 2 O) 2 ]) have contact during the life‐time of the excited state, but static quenching refers to complex formation between fluorophore–quencher …”

Section: Resultsmentioning

confidence: 99%

“…quencher. [21] The mechanisms of fluorescence quenching (static and dynamic) could be distinguished experimentally through change in the HSA absorption spectrum and temperature dependence of the quenching constant. The higher temperatures will cause faster diffusion and larger amounts of collisional quenching for dynamic quenching and the quenching constant values will increase with increasing temperature,…”

Section: Uv-spectrophotometrymentioning

confidence: 99%

Interaction studies of copper complex containing food additive carmoisine dye with human serum albumin (HSA): Spectroscopic investigations

et al. 2017

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In this study, the interaction between human serum albumin (HSA) and a copper complex of carmoisine dye; [Cu(carmoisine) (H O) ], was studied in vitro using multi-spectroscopic methods. It was found that the intrinsic fluorescence of HSA was quenched by the addition of the [Cu(carmoisine) (H O) ] complex and the quenching mechanism was considered as static quenching by formation of a [Cu(carmoisine) (H O) ]-HSA complex. The binding constant was about 10 M at room temperature. The values of the calculated thermodynamic parameters (ΔH < 0 and ΔS > 0) suggested that both hydrogen bonds and the hydrophobic interactions were involved in the binding process. The site marker competitive experiments revealed that the binding of [Cu(carmoisine) (H O) ] to HSA primarily occurred in subdomain IIIA (site II) of HSA. The results of circular dichroism (CD) and UV-vis spectroscopy showed that the micro-environment of amino acid residues and the conformation of HSA were changed after addition of the [Cu(carmoisine) (H O) ] complex. Finally, the binding of the [Cu(carmoisine) (H O) ] complex to HSA was modelled by a molecular docking method. Excellent agreement was obtained between the experimental and theoretical results with respect to the binding forces and binding constant.

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“…Therefore, a hydrophobic portion of surfactant participated in the associations of protein molecules which resulted in the formation of amorphous aggregate. At room temperature (25°C) and pH 7.5, no aggregation process took place, as shown in S3 Fig [ 64 ], and there is no interferences were found with respect to the buffer used in the experiments ( S4 Fig ). On the other side, at pH 3.5 no interaction was found between surfactant and albumins due to electrostatic repulsion.…”

Section: Resultsmentioning

confidence: 99%

Rosin Surfactant QRMAE Can Be Utilized as an Amorphous Aggregate Inducer: A Case Study of Mammalian Serum Albumin

et al. 2015

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Quaternary amine of diethylaminoethyl rosin ester (QRMAE), chemically synthesized biocompatible rosin based cationic surfactant, has various biological applications including its use as a food product additive. In this study, we examined the amorphous aggregation behavior of mammalian serum albumins at pH 7.5, i.e., two units above their isoelectric points (pI ~5.5), and the roles played by positive charge and hydrophobicity of exogenously added rosin surfactant QRMAE. The study was carried out on five mammalian serum albumins, using various spectroscopic methods, dye binding assay, circular dichroism and electron microscopy. The thermodynamics of the binding of mammalian serum albumins to cationic rosin modified surfactant were established using isothermal titration calorimetry (ITC). It was observed that a suitable molar ratio of protein to QRMAE surfactant enthusiastically induces amorphous aggregate formation at a pH above two units of pI. Rosin surfactant QRMAE-albumins interactions revealed a unique interplay between the initial electrostatic and the subsequent hydrophobic interactions that play an important role towards the formation of hydrophobic interactions-driven amorphous aggregate. Amorphous aggregation of proteins is associated with varying diseases, from the formation of protein wine haze to the expansion of the eye lenses in cataract, during the expression and purification of recombinant proteins. This study can be used for the design of novel biomolecules or drugs with the ability to neutralize factor(s) responsible for the aggregate formation, in addition to various other industrial applications.

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Interaction of biocompatible natural rosin-based surfactants with human serum albumin: A biophysical study

Cited by 28 publications

References 56 publications

Binding modes of environmental endocrine disruptors to human serum albumin: insights from STD-NMR, ITC, spectroscopic and molecular docking studies

Binding modes of environmental endocrine disruptors to human serum albumin: insights from STD-NMR, ITC, spectroscopic and molecular docking studies

Interaction studies of copper complex containing food additive carmoisine dye with human serum albumin (HSA): Spectroscopic investigations

Rosin Surfactant QRMAE Can Be Utilized as an Amorphous Aggregate Inducer: A Case Study of Mammalian Serum Albumin

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