Giannousi, K;
Geromichalos, G;
Kakolyri, D;
Mourdikoudis, S;
Dendrinou-Samara, C;
(2020)
Interaction of ZnO Nanostructures with Proteins: In Vitro Fibrillation/Antifibrillation Studies and in Silico Molecular Docking Simulations.
ACS Chemical Neuroscience
, 11
(3)
pp. 436-444.
10.1021/acschemneuro.9b00642.
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Abstract
Protein amyloidosis is related to many neurological disorders. Nanoparticles (NPs) due to their small size can regulate both the polypeptide monomers/oligomers assembly into amyloid fibrils/plaques and the disintegration of the existent plaques. Herein, we have synthesized ZnO nanoflowers and polyol-coated ZnO NPs of relatively small size (40 nm) with cylindrical shape, through solvothermal and microwave-assisted routes, respectively. The effect of the different morphology of nanostructures on the fibrillation/antifibrillation process was monitored in bovine serum albumin (BSA) and human insulin (HI) by fluorescence Thioflavin T (ThT) measurements. Although both nanomaterials affected the amyloid formation mechanism as well as their disaggregation, ZnO nanoflowers with their sharp edges exhibited the greatest amyloid degradation rate in both model proteins (73% and 35%, respectively) and inhibited the most the insulin fibril growth, while restrained also the fibrillation process in the case of albumin solution. In silico molecular docking simulations on the crystal structure of BSA and HI were performed to analyze further the observed in vitro activity of ZnO nanostructures. The binding energy of ZnO NPs was found lower for BSA (−5.44), highlighting their ability to act as catalysts in the fibrillation process of albumin monomers.
| Type: | Article |
|---|---|
| Title: | Interaction of ZnO Nanostructures with Proteins: In Vitro Fibrillation/Antifibrillation Studies and in Silico Molecular Docking Simulations |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1021/acschemneuro.9b00642 |
| Publisher version: | https://doi.org/10.1021/acschemneuro.9b00642 |
| Language: | English |
| Additional information: | This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions. |
| Keywords: | Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, Chemistry, Medicinal, Neurosciences, Pharmacology & Pharmacy, Neurosciences & Neurology, ZnO, nanoflowers, albumin, insulin, fibrillation/antifibrillation, in silico, ZINC-OXIDE NANOPARTICLES, SERUM-ALBUMIN, BOVINE, AGGREGATION, INSULIN, ELUCIDATION, MECHANISM, TOXICITY, LYSOZYME |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > UCL BEAMS UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Physics and Astronomy |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10093321 |
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