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Emergence of visible light optical properties of L-phenylalanine aggregates

The ability of phenylalanine to form fibrillar nanostructures was demonstrated on multiple occasions, and such an oligomerization reaction could be the cause of cytotoxicity in patients with phenylketonuria. These findings were supported by claims that L-phenylalanine (Phe) fibrils have amyloid prop...

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Autores principales: Ziaunys, Mantas, Smirnovas, Vytautas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6394350/
https://www.ncbi.nlm.nih.gov/pubmed/30828498
http://dx.doi.org/10.7717/peerj.6518
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author Ziaunys, Mantas
Smirnovas, Vytautas
author_facet Ziaunys, Mantas
Smirnovas, Vytautas
author_sort Ziaunys, Mantas
collection PubMed
description The ability of phenylalanine to form fibrillar nanostructures was demonstrated on multiple occasions, and such an oligomerization reaction could be the cause of cytotoxicity in patients with phenylketonuria. These findings were supported by claims that L-phenylalanine (Phe) fibrils have amyloid properties and can be detected using thioflavin T fluorescence assay. However, a part of Phe aggregation studies reported the opposite data, suggesting no amyloid structures to be formed. Due to the contradicting reports, the amyloid nature of Phe aggregates remains uncertain. In this work we tested Phe aggregation under conditions where amyloid formation was previously reported. We show the emergence of Phe aggregates with visible light optical properties that overlap with the spectra of dyes used in amyloid fibril assays, which could lead to false-positive identifications.
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spelling pubmed-63943502019-03-01 Emergence of visible light optical properties of L-phenylalanine aggregates Ziaunys, Mantas Smirnovas, Vytautas PeerJ Biochemistry The ability of phenylalanine to form fibrillar nanostructures was demonstrated on multiple occasions, and such an oligomerization reaction could be the cause of cytotoxicity in patients with phenylketonuria. These findings were supported by claims that L-phenylalanine (Phe) fibrils have amyloid properties and can be detected using thioflavin T fluorescence assay. However, a part of Phe aggregation studies reported the opposite data, suggesting no amyloid structures to be formed. Due to the contradicting reports, the amyloid nature of Phe aggregates remains uncertain. In this work we tested Phe aggregation under conditions where amyloid formation was previously reported. We show the emergence of Phe aggregates with visible light optical properties that overlap with the spectra of dyes used in amyloid fibril assays, which could lead to false-positive identifications. PeerJ Inc. 2019-02-25 /pmc/articles/PMC6394350/ /pubmed/30828498 http://dx.doi.org/10.7717/peerj.6518 Text en © 2019 Ziaunys and Smirnovas http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited.
spellingShingle Biochemistry
Ziaunys, Mantas
Smirnovas, Vytautas
Emergence of visible light optical properties of L-phenylalanine aggregates
title Emergence of visible light optical properties of L-phenylalanine aggregates
title_full Emergence of visible light optical properties of L-phenylalanine aggregates
title_fullStr Emergence of visible light optical properties of L-phenylalanine aggregates
title_full_unstemmed Emergence of visible light optical properties of L-phenylalanine aggregates
title_short Emergence of visible light optical properties of L-phenylalanine aggregates
title_sort emergence of visible light optical properties of l-phenylalanine aggregates
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6394350/
https://www.ncbi.nlm.nih.gov/pubmed/30828498
http://dx.doi.org/10.7717/peerj.6518
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