Please use this identifier to cite or link to this item: http://hdl.handle.net/2080/4203
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dc.contributor.authorJena, Sonali-
dc.contributor.authorJha, Suman-
dc.date.accessioned2023-12-28T12:50:09Z-
dc.date.available2023-12-28T12:50:09Z-
dc.date.issued2023-12-
dc.identifier.citation92nd Annual Meet of the Society of Biological Chemists(SBC) BITS Pilani, 18-20th Dec 2023en_US
dc.identifier.urihttp://hdl.handle.net/2080/4203-
dc.descriptionCopyright belongs to proceeding publisheren_US
dc.description.abstractParkinson's disease (PD) is a progressive neurodegenerative disorder, characterized by the degeneration of dopaminergic neurons in the substantia nigra and the abnormal accumulation of Alpha-synuclein (α-syn) aggregates or Lewy bodies, leading to a major loss of motor function. α-Syn is an intrinsically disordered protein, involved in vesicular trafficking and neurotransmitter release. The aggregation of α-syn involves a cascade of structural transition from monomeric protein to the fibrillar form of protein, which is known to be a complex process and is regulated by several intrinsic and extrinsic factors. Currently, nanoparticles have been reported for easy drug delivery as they can easily pass the blood-brain barrier. There are several reports suggesting that the interfaces of metal oxide nanoparticles have a direct effect on α-syn conformation, and it can inhibit the protein amyloidogenesis. Hence, in this report, we screen different ZnONP interfaces (chemically and biologically synthesized) with anti-amyloidogenic potential for α-synen_US
dc.subjectCoronaen_US
dc.subjectα-synucleinen_US
dc.titleCorona of Biologically Synthesized Nanoparticle Provide Better Interface to Trap Monomeric Α-Synuclein in Non-Cytotoxic Amorphous Aggregate Structureen_US
dc.typePresentationen_US
Appears in Collections:Conference Papers

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