Amyloid like aggregates formed by the self-assembly of proline and hydroxyproline

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dc.contributor.author Koshti, Bharti
dc.contributor.author Chilwal, Ramesh Singh
dc.contributor.author Kshtriya, Vivekshinh
dc.contributor.author Walia, Shanka
dc.contributor.author Bhatia, Dhiraj
dc.contributor.author Joshi, K. B.
dc.contributor.author Gour, Nidhi
dc.date.accessioned 2021-02-05T14:54:03Z
dc.date.available 2021-02-05T14:54:03Z
dc.date.issued 2021-01
dc.identifier.citation Koshti, Bharti; Chilwal, Ramesh Singh; Kshtriya, Vivekshinh; Walia, Shanka; Bhatia, Dhiraj; Joshi, K. B. and Gour, Nidhi , "Amyloid like aggregates formed by the self-assembly of proline and hydroxyproline", ChemRxiv.org, DOI: 10.26434/chemrxiv.13615385.v1, Jan. 2021. en_US
dc.identifier.uri http://dx.doi.org/10.26434/chemrxiv.13615385.v1
dc.identifier.uri https://repository.iitgn.ac.in/handle/123456789/6266
dc.description.abstract Single amino acid based self-assembled structures have gained a lot of interest recently owing to their pathological significance in metabolite disorders. There is plethora of significant research work which illustrate amyloid like characteristics of assemblies formed by aggregation of single amino acids like Phenylalanine, Tyrosine, Tryptophan, Cysteine and Methionine and its implications in pathophysiology of single amino acid metabolic disorders like phenylketonuria, tyrosinemia, hypertryptophanemia, cystinuria and hypermethioninemia respectively. Hence, studying aggregation behaviour of single amino acids is very crucial to assess the underlying molecular mechanism behind metabolic disorders. In this manuscript we report for the very first time the aggregation properties of non-aromatic single amino acids Hydroxy-proline and Proline. The morphologies of these were studied extensively by Optical microscopy (OM), ThT binding fluorescence microscopy, Scanning Electron Microscopy (SEM) and Atomic force microscopy (AFM). It can be assessed that these amino acids form globular structures at lower concentrations and gradually changes to tape like structures on increasing the concentration as assessed by AFM. ThT and CR binding assay reveal the aggregates do have amyloid like characteristics. Further MTT assays on SHSY5Y neural cell lines reveal cytotoxicity and the aggregates caused significant cell death in dose dependent manner. These results have important implications in understanding the pathophysiology of single amino acid disorders like Hyperprolinemia and Hydroxyprolinemia in association with amyloid diseases. The symptoms of these diseases are also accompanied by extensive neurological problems like intellectual disability, seizures and psychiatric problems which further evince amyloid like etiology for these rare in-born errors of metabolism.
dc.description.statementofresponsibility by Bharti Koshti, Ramesh Singh Chilwal, VivekshinhKshtriya, Shanka Walia, Dhiraj Bhatia, K. B. Joshi and Nidhi Gour
dc.language.iso en_US en_US
dc.publisher ChemRxiv.org en_US
dc.title Amyloid like aggregates formed by the self-assembly of proline and hydroxyproline en_US
dc.type Pre-Print en_US
dc.relation.journal ChemRxiv


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