Please use this identifier to cite or link to this item: http://hdl.handle.net/2080/4113
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dc.contributor.authorMohanty, Sonali-
dc.contributor.authorBhattacharyya, Dipita-
dc.contributor.authorSingh, Ajit Kumar-
dc.contributor.authorJena, Sonali-
dc.contributor.authorMahakud, Amaresh Kumar-
dc.contributor.authorBhunia, Anirban-
dc.contributor.authorJha, Anupam Nath-
dc.contributor.authorSaleem, Mohammed-
dc.contributor.authorJha, Suman-
dc.date.accessioned2023-12-01T05:27:52Z-
dc.date.available2023-12-01T05:27:52Z-
dc.date.issued2023-11-
dc.identifier.citation3rd International Conference on Nanomaterials in Biology, IIT Gandhinagar, India, 19-22 November 2023en_US
dc.identifier.urihttp://hdl.handle.net/2080/4113-
dc.descriptionCopyright belongs to proceeding publisheren_US
dc.description.abstractParkinson’s disease is a progressive neurodegenerative disorder associated with aggregation of α-synuclein (αS), resulting in formation of plaques in neurons described as Lewy bodies. α-synuclein is a small, soluble, and intrinsically disordered protein that upon gaining amyloidogenic conformation forms rigid cross-β sheet structure with fibril-like morphology via cytotoxic oligomeric intermediates. In recent years, nanoparticles have gained momentum due to their nano-size and large surface to volume ratio. The binding of α-synuclein onto nanoparticle surface is likely to induce conformational rearrangements, thereby anticipated to impede them in folding pathways and affect overall bio-reactivity of nanoparticle. In this subject, our study explores the positive and negative interface interaction of zinc oxide nanoparticle (ZnONP) with α-synuclein, and its following impact on protein fibrillation kinetics and fibril mediated cytotoxicity. The interaction studies of -synuclein monomer and ZnONPs interface at higher concentration is indicative of multi-layered adsorption of α-synuclein or significant rearrangement in protein orientation that ensures tight packaging leading to inhibition of protein fibrillation. Further, TEM micrographs of ZnONP complexed α-synuclein shows mesh like pattern as compared to fibril like structure found in wild type α-synuclein. Impressively, α-synuclein complexed with ZnONP shows remarkably lowered cytotoxicity against the SH-SY-5Y and THP-1 cells in-vitro, as compared to aggregated α-synuclein. Henceforth, this study provides new insight on the therapeutic potential of ZnONP in combating pathologies related to α-synuclein aggregation.en_US
dc.subjectProtein aggregationen_US
dc.subjectNanoparticleen_US
dc.subjectInteraction profileen_US
dc.subjectFibrillation kineticsen_US
dc.subjectFibrillation kineticsen_US
dc.titleConformational Dynamics of Α-Synuclein in Presence of Bare and Surface Functionalized Znonpsen_US
dc.typePresentationen_US
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