Fluorescence study on the interaction of human serum albumin with Butein in liposomes

Toprak, Mahmut

doi:10.1016/j.saa.2015.10.023

Cited by 35 publications

(10 citation statements)

References 32 publications

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“…Fluorescence quenching is a useful approach to get insight into the understanding of the interaction of compounds of several sources with body proteins [ 49 ]. Thus, fluorescence quenching has been used to measure the binding affinities between the liposomes and BSA.…”

Section: Resultsmentioning

confidence: 99%

Evidence of Protein Adsorption in Pegylated Liposomes: Influence of Liposomal Decoration

et al. 2017

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In order to contribute to a better knowledge of the events involved in the formation of the protein corona when nanoparticles (NPs) come in contact with proteins, we report a study about the changes on the physicochemical properties of pristine, PEGylated and Cyclic Arginine-Glycine-Aspartate peptide (RGD)-functionalized large unilamelar liposomes (LUVs) or magnetoliposomes (MLs) upon incubation with Bovine Serum Albumin (BSA). The main phospholipid component of both LUVs and MLs was l-α-phosphatydylcholine (PC) or 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) with 20% of cholesterol. The most obvious indication of the interaction of BSA-nanosystems is given by changes in the hydrodynamic diameter of the particles but other evidence is needed to corroborate the process. Our findings indicate that size modification is a process that is accomplished in few hours and that is strongly dependent not only on the surface decoration but also of the lipid composition of both LUVs and MLs. Fluorescence quenching experiments as well as cryogenic transmission electron microscopy (Cryo-TEM) images assessed these changes and confirmed that although each system has to be studied in a particular way, we can establish three distinctive features that turn into more reactive systems: (a) compositions containing PC compared with their DMPC counterparts; (b) the presence of PEG and/or RGD compared to the pristine counterparts; and (c) the presence of SPIONs: MLs show higher interaction than LUVs of the same lipid composition. Consequently, PEGylation (that is supposed to make stealth NPs) actually fails in preventing complete protein binding.

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Section: Resultsmentioning

confidence: 99%

Evidence of Protein Adsorption in Pegylated Liposomes: Influence of Liposomal Decoration

et al. 2017

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“…It is theorised that the primary quenching mechanism behind these fluorescent responses is ground-state complexation, in which the chiral analyte associates with the BINOL moieties in the framework prior to excitation and forms a non-emissive complex. 19 Time-resolved fluorescence experiments, including excited-state lifetime studies, are required to confirm this proposed static quenching mechanism.…”

mentioning

confidence: 99%

A chiral binaphthyl-based coordination polymer as an enantioselective fluorescence sensor

2022

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“…By comparing the fluorescence spectra before and after the binding of biological macromolecules to other molecules, it is possible to infer the binding constant (K a ), number of binding sites (n), and thermodynamic parameters between the molecules. 13 Figure 4 demonstrates the effect of engeletin on the fluorescence spectrum of α-glucosidase. With increasing concentration of engeletin, the fluorescence intensity gradually decreased, confirming the existence of an interaction between engeletin and α-glucosidase.…”

Section: Resultsmentioning

confidence: 99%

Inhibitory Mechanism of Engeletin Against α-Glucosidase

Liu

Zhou

et al. 2021

Natural Product Communications

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The inhibitory mechanism of engeletin against α-glucosidase was investigated for the first time by fluorescence spectroscopy and molecular docking. The results showed that engeletin could inhibit α-glucosidase in a noncompetitive inhibition mode with a half-maximal inhibitory concentration value of 48.5 ± 6.0 µg/mL (0.11 ± 0.014 mmol/L). It was found that engeletin could cause static fluorescence quenching of α-glucosidase by forming a complex with α-glucosidase. The thermodynamic parameters indicated that the combination of engeletin and α-glucosidase was driven by hydrophobic force. The molecular docking results confirmed that some amino acid residues of α-glucosidase (Trp391, Arg428, Glu429, Gly566, Trp710, Glu771) could interact with engeletin by hydrogen bonding.

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Fluorescence study on the interaction of human serum albumin with Butein in liposomes

Cited by 35 publications

References 32 publications

Evidence of Protein Adsorption in Pegylated Liposomes: Influence of Liposomal Decoration

Evidence of Protein Adsorption in Pegylated Liposomes: Influence of Liposomal Decoration

A chiral binaphthyl-based coordination polymer as an enantioselective fluorescence sensor

Inhibitory Mechanism of Engeletin Against α-Glucosidase

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