Please use this identifier to cite or link to this item:
http://hdl.handle.net/2080/4113
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Mohanty, Sonali | - |
dc.contributor.author | Bhattacharyya, Dipita | - |
dc.contributor.author | Singh, Ajit Kumar | - |
dc.contributor.author | Jena, Sonali | - |
dc.contributor.author | Mahakud, Amaresh Kumar | - |
dc.contributor.author | Bhunia, Anirban | - |
dc.contributor.author | Jha, Anupam Nath | - |
dc.contributor.author | Saleem, Mohammed | - |
dc.contributor.author | Jha, Suman | - |
dc.date.accessioned | 2023-12-01T05:27:52Z | - |
dc.date.available | 2023-12-01T05:27:52Z | - |
dc.date.issued | 2023-11 | - |
dc.identifier.citation | 3rd International Conference on Nanomaterials in Biology, IIT Gandhinagar, India, 19-22 November 2023 | en_US |
dc.identifier.uri | http://hdl.handle.net/2080/4113 | - |
dc.description | Copyright belongs to proceeding publisher | en_US |
dc.description.abstract | Parkinson’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.subject | Protein aggregation | en_US |
dc.subject | Nanoparticle | en_US |
dc.subject | Interaction profile | en_US |
dc.subject | Fibrillation kinetics | en_US |
dc.subject | Fibrillation kinetics | en_US |
dc.title | Conformational Dynamics of Α-Synuclein in Presence of Bare and Surface Functionalized Znonps | en_US |
dc.type | Presentation | en_US |
Appears in Collections: | Conference Papers |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
2023_ICNB_SMohanty_Conformationa.pdf | 2.03 MB | Adobe PDF | View/Open Request a copy |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.