Unusual aggregates formed by the self-assembly of proline, hydroxyproline, and lysine

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dc.contributor.author Koshti, Bharti
dc.contributor.author Kshtriya, Vivekshinh
dc.contributor.author Singh, Ramesh
dc.contributor.author Walia, Shanka
dc.contributor.author Bhatia, Dhiraj
dc.contributor.author Joshi, Khashti Ballabh
dc.contributor.author Gour, Nidhi
dc.coverage.spatial United States of America
dc.date.accessioned 2012-10-04T17:16:06Z
dc.date.available 2012-10-04T17:16:06Z
dc.date.issued 2021-09
dc.identifier.citation Koshti, Bharti; Kshtriya, Vivekshinh; Singh, Ramesh; Walia, Shanka; Bhatia, Dhiraj; Joshi, Khashti Ballabh and Gour, Nidhi, "Unusual aggregates formed by the self-assembly of proline, hydroxyproline, and lysine", ACS Chemical Neuroscience, DOI: 10.1021/acschemneuro.1c00427, vol. 12, no. 17, pp. 3237-3249, Sep. 2021. en_US
dc.identifier.issn 1948-7193
dc.identifier.uri https://doi.org/10.1021/acschemneuro.1c00427
dc.identifier.uri https://repository.iitgn.ac.in/handle/123456789/6842
dc.description.abstract There is a plethora of significant research that illustrates toxic self-assemblies formed by the aggregation of single amino acids, such as phenylalanine, tyrosine, tryptophan, cysteine, and methionine, and their implication on the etiology of inborn errors of metabolisms (IEMs), such as phenylketonuria, tyrosinemia, hypertryptophanemia, cystinuria, and hypermethioninemia, respectively. Hence, studying the aggregation behavior of single amino acids is very crucial from the chemical neuroscience perspective to understanding the common etiology between single amino acid metabolite disorders and amyloid diseases like Alzheimer's and Parkinson's. Herein we report the aggregation properties of nonaromatic single amino acids L-proline (Pro), L-hydroxyproline (Hyp), and L-lysine hydrochloride (Lys). The morphologies of the self-assembled structures formed by Pro, Hyp, and Lys were extensively studied by various microscopic techniques, and controlled morphological transitions were observed under varied concentrations and aging times. The mechanism of structure formation was deciphered by concentration-dependent 1H NMR analysis, which revealed the crucial role of hydrogen bonding and hydrophobic interactions in the structure formation of Pro, Hyp, and Lys. MTT assays on neural (SHSY5Y) cell lines revealed that aggregates formed by Pro, Hyp, and Lys reduced cell viability in a dose-dependent manner. These results may have important implications in the understanding of the patho-physiology of disorders such as hyperprolinemia, hyperhydroxyprolinemia, and hyperlysinemia since all these IEMs are associated with severe neurodegenerative symptoms, including intellectual disability, seizures, and psychiatric problems. Our future studies will endeavor to study these biomolecular assemblies in greater detail by immuno-histochemical analysis and advanced biophysical assays.
dc.description.statementofresponsibility by Bharti Koshti, Vivekshinh Kshtriya, Ramesh Singh, Shanka Walia, Dhiraj Bhatia, Khashti Ballabh Joshi and Nidhi Gour
dc.format.extent vol. 12, no. 17, pp. 3237-3249
dc.language.iso en_US en_US
dc.publisher American Chemical Society en_US
dc.subject Chemical structure en_US
dc.subject Self organization en_US
dc.subject Assays en_US
dc.subject Peptides en_US
dc.subject Proteins en_US
dc.subject Monomers en_US
dc.title Unusual aggregates formed by the self-assembly of proline, hydroxyproline, and lysine en_US
dc.type Article en_US
dc.relation.journal ACS Chemical Neuroscience

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