Interaction of ANS with human serum albumin under confinement: Important insights and relevance

Malik, Ashima; Kundu, Jayanta; Karmakar, Sandip; Lai, Sima; Chowdhury, P. K.

doi:10.1016/j.jlumin.2015.06.034

Cited by 6 publications

(6 citation statements)

References 42 publications

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“…In the case of co‐encapsulated liposome, the fluorescence intensity increased – much higher than that of the unloaded or single loaded liposome – indicating that the co‐encapsulation could further decrease the fluidity of liposomal membrane, implying the capability to improve the stability of the liposomes, which was consistent with the results of DSC. It was also found that the emission band remarkably shifted to a longer wavelength, suggesting the variation of the polar conditions in the hydrophobic cavity; that is, it experienced a more polar microenvironment in the bilayer membrane as compared to that in the un‐L and single loaded liposome 35 …”

Section: Resultsmentioning

confidence: 98%

Physicochemical properties, antioxidant activities and in vitro sustained release behaviour of co‐encapsulated liposomes as vehicle for vitamin E and β‐carotene

Zhang

Cheng

et al. 2022

J Sci Food Agric

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BACKGROUND In this study the potential of liposomes as a vitamin E (VE) and β‐carotene (βC) delivery system was examined. The co‐encapsulated liposomes of βC and VE (L‐VE‐βC) were prepared and characterized. Their antioxidant properties were evaluated by free radical scavenging activities of 2,2‐diphenyl‐1‐picrylhydrazyl (DPPH), 2,2′‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulfonic acid (ABTS), hydroxyl radical and lipid peroxidation assay. The in vitro sustained release behaviour was then investigated and discussed. RESULTS VE and βC were co‐encapsulated in liposomes with high encapsulation efficiency, up to 92.49% and 86.16% for βC and VE, respectively. The antioxidant activities of L‐VE‐βC samples were significantly higher than that of single loaded liposome. Among different ratios of VE/βC, L‐VE‐βC at 5:3 exhibited the highest radical scavenging rates, with 66.80%, 56.58% and 34.39% for DPPH, ABTS and OH radical, respectively. L‐VE‐βC samples also had a good ability to inhibit lipid peroxidation, especially the sample with ratios of VE/βC at 5:3 and 3:1. In simulated gastrointestinal release, L‐VE‐βC exhibited an excellent sustained release behaviour in SGF with the accumulated rate at about 20%, while the release rate in SIF increased to over 80%, where they should be absorbed. The release kinetics analysis indicated that βC was released in the Higuchi model in stomach, and the Korsmeyr–Peppas model in intestine. CONCLUSION Compared to single loaded liposomes, the combined‐loaded liposomes exhibited higher antioxidant activity and bioavailability, suggesting the potential applications in functional foods. © 2022 Society of Chemical Industry.

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Section: Resultsmentioning

confidence: 98%

Physicochemical properties, antioxidant activities and in vitro sustained release behaviour of co‐encapsulated liposomes as vehicle for vitamin E and β‐carotene

Zhang

Cheng

et al. 2022

J Sci Food Agric

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“…The longer lifetime (τ 2 ) can be assigned to the molecular species totally confined in the hydrophobic pockets and shorter lifetime (τ 1 ) can be assigned to the molecular species bound to the hydrophobic pockets, partially exposed to water molecules. According to previous studies, [48][49][50] the former hydrophobic pockets could be assigned to one in subdomains IIA and IIIA located at the protein inside with high affinity and the latter may be in the domain I near the protein surface, as described in Supporting information 2. increases. This result shows that as the concentration increases, numbers of ANS molecules at binding sites near protein surface decrease, while those inside the hydrophobic pockets increase.…”

Section: Fluorescence Lifetime Analysis Of Ans In Bsa Solutions and Tmentioning

confidence: 93%

“…From previous studies, the primary binding sites of BSA are located at hydrophobic pockets in a few parts of subdomain, thus, the hydrophobic pockets of BSA can be expected as a hydrophobic nanosized gap and work as a good model system of intramolecular confinement environment. [48][49][50] Therefore, BSA concentration dependence of ANS fluorescence was carried out as a model system. to 300 mg/ml, respectively.…”

Section: Ans Fluorescence Spectra At Various Concentrations Of Bsamentioning

confidence: 99%

Spectroscopic Analysis of Protein‐Crowded Environments Using the Charge‐Transfer Fluorescence Probe 8‐Anilino‐1‐Naphthalenesulfonic Acid

Ota

Takano

2019

ChemPhysChem

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The molecular behaviors of proteins under crowding conditions are crucial for understanding the protein actions in intracellular environments. Under a crowded environment, the distance between protein molecules is almost the same size as the molecular level, thus, both the excluded volume effect and short ranged soft chemical interaction on protein surface could induce the complicated influence on the protein behavior cooperatively. Recently, various kinds of analytical approaches from macroscopic to microscopic aspects have been made to evaluate the crowding effect. The method, however, has not been established to evaluate the surface specific interactions on protein surface. In this study, the analytical method to evaluate the crowding effect has been suggested by using a charge‐transfer fluorescence probe, ANS. By employing the unique property of ANS attaching to charged residues on the surface of lysozyme, the crowding effect was focused, while the case was compared as a reference, in which ANS is confined in hydrophobic pockets of BSA. Consequently, the surface specific changes of fluorescence spectra were readily observed under the crowded environment, whereas the fluorescence spectra of ANS in protein inside did not change. This result suggests the fluorescence spectra of ANS binding to protein surface have the capability to estimate the crowding effect of proteins.

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“…[18][19][20][21][22][23][24] Malik et al studied the interaction of 1-anilinonapthelenesulfonate (ANS) with HSA under confinement and reported that the binding of ANS to HSA in AOT reverse micelles is significantly retarded as compared to in a buffer and suggested the non-specificity of domain specific binding sites in the reverse micellar system as the probable reason. 25 It has been generally confirmed that proteins behave differently in confined environments as compared to in bulk. 21,22,24,25 Considering the idea of confinement, it is expected that proteins will undergo faster conformational dynamics in a confined environment due to restriction of the free movement of the polypeptide chains, and the effect of temperature should also be less prominent under confinement compared to that in bulk.…”

Section: Introductionmentioning

confidence: 95%

“…25 It has been generally confirmed that proteins behave differently in confined environments as compared to in bulk. 21,22,24,25 Considering the idea of confinement, it is expected that proteins will undergo faster conformational dynamics in a confined environment due to restriction of the free movement of the polypeptide chains, and the effect of temperature should also be less prominent under confinement compared to that in bulk.…”

Section: Introductionmentioning

confidence: 95%

Startling temperature effect on proteins when confined: single molecular level behaviour of human serum albumin in a reverse micelle

Sengupta

Yadav

Sen

2016

Phys. Chem. Chem. Phys.

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The present work reports the effect of confinement, and temperature therein, on the conformational fluctuation dynamics of domain-I of human serum albumin (HSA) by fluorescence correlation spectroscopy (FCS). The water-pool of a sodium bis(2-ethylhexyl)sulfosuccinate (AOT) reverse micelle has been used as the confined environment. It was observed that the conformational fluctuation time is about 6 times smaller compared to bulk medium when confined in a water-pool of 3.5 nm radius. On increasing the size of the water-pool the conformational fluctuation time was found to increase monotonically and approaches the bulk value. The effect of confinement is on par with the general belief about the restricted motion of a macromolecule upon confinement. However, the effect of temperature was found to be surprising. An increase in the temperature from 298 K to 313 K induces a larger change in the conformational fluctuation time in HSA, when confined. In the bulk medium, apparently there is no change in the conformational fluctuation time in the aforementioned temperature range, whereas, when HSA is present in an AOT water-pool of radius 3.5 nm, about an 88% increase in the fluctuation time was observed. The observed prominent thermal effect on the conformational dynamics of domain-I of HSA in the water-pool of an AOT reverse micelle as compared to in the bulk medium was concluded to arise from the confined solvent effect.

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Interaction of ANS with human serum albumin under confinement: Important insights and relevance

Cited by 6 publications

References 42 publications

Physicochemical properties, antioxidant activities and in vitro sustained release behaviour of co‐encapsulated liposomes as vehicle for vitamin E and β‐carotene

Physicochemical properties, antioxidant activities and in vitro sustained release behaviour of co‐encapsulated liposomes as vehicle for vitamin E and β‐carotene

Spectroscopic Analysis of Protein‐Crowded Environments Using the Charge‐Transfer Fluorescence Probe 8‐Anilino‐1‐Naphthalenesulfonic Acid

Startling temperature effect on proteins when confined: single molecular level behaviour of human serum albumin in a reverse micelle

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