Cargando…

Novel, Inexpensive, and Scalable Amyloid Fibril Formation Method

Wheat flour was used as a source of protein for the in vitro synthesis of Amyloid fibrils to develop a novel and inexpensive fabrication method. Amyloid fibrillation was confirmed by Thioflavin T Fluorescence, using confocal microscopy. A morphological study was carried out by transmission electron...

Descripción completa

Detalles Bibliográficos
Autores principales: Hessick, Ethan, Pawar, Milind, Souchereau, Reid, Schmitz, Emma, Gouma, Pelagia-Irene
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8911616/
https://www.ncbi.nlm.nih.gov/pubmed/35268997
http://dx.doi.org/10.3390/ma15051766
_version_ 1784666862324285440
author Hessick, Ethan
Pawar, Milind
Souchereau, Reid
Schmitz, Emma
Gouma, Pelagia-Irene
author_facet Hessick, Ethan
Pawar, Milind
Souchereau, Reid
Schmitz, Emma
Gouma, Pelagia-Irene
author_sort Hessick, Ethan
collection PubMed
description Wheat flour was used as a source of protein for the in vitro synthesis of Amyloid fibrils to develop a novel and inexpensive fabrication method. Amyloid fibrillation was confirmed by Thioflavin T Fluorescence, using confocal microscopy. A morphological study was carried out by transmission electron microscopy (TEM), which revealed the high aspect ratio of the amyloid fibrils formed via a novel process. An application of the amyloid fibers produced by the novel method is shown to be melatonin sensing. Tests showed that the amyloid samples had a measurable color variation dependent on the melatonin concentration. This newly derived process could prove to be a cost-effective tool for future nano-biomaterial applications in commercial and research settings.
format Online
Article
Text
id pubmed-8911616
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-89116162022-03-11 Novel, Inexpensive, and Scalable Amyloid Fibril Formation Method Hessick, Ethan Pawar, Milind Souchereau, Reid Schmitz, Emma Gouma, Pelagia-Irene Materials (Basel) Article Wheat flour was used as a source of protein for the in vitro synthesis of Amyloid fibrils to develop a novel and inexpensive fabrication method. Amyloid fibrillation was confirmed by Thioflavin T Fluorescence, using confocal microscopy. A morphological study was carried out by transmission electron microscopy (TEM), which revealed the high aspect ratio of the amyloid fibrils formed via a novel process. An application of the amyloid fibers produced by the novel method is shown to be melatonin sensing. Tests showed that the amyloid samples had a measurable color variation dependent on the melatonin concentration. This newly derived process could prove to be a cost-effective tool for future nano-biomaterial applications in commercial and research settings. MDPI 2022-02-26 /pmc/articles/PMC8911616/ /pubmed/35268997 http://dx.doi.org/10.3390/ma15051766 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Hessick, Ethan
Pawar, Milind
Souchereau, Reid
Schmitz, Emma
Gouma, Pelagia-Irene
Novel, Inexpensive, and Scalable Amyloid Fibril Formation Method
title Novel, Inexpensive, and Scalable Amyloid Fibril Formation Method
title_full Novel, Inexpensive, and Scalable Amyloid Fibril Formation Method
title_fullStr Novel, Inexpensive, and Scalable Amyloid Fibril Formation Method
title_full_unstemmed Novel, Inexpensive, and Scalable Amyloid Fibril Formation Method
title_short Novel, Inexpensive, and Scalable Amyloid Fibril Formation Method
title_sort novel, inexpensive, and scalable amyloid fibril formation method
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8911616/
https://www.ncbi.nlm.nih.gov/pubmed/35268997
http://dx.doi.org/10.3390/ma15051766
work_keys_str_mv AT hessickethan novelinexpensiveandscalableamyloidfibrilformationmethod
AT pawarmilind novelinexpensiveandscalableamyloidfibrilformationmethod
AT souchereaureid novelinexpensiveandscalableamyloidfibrilformationmethod
AT schmitzemma novelinexpensiveandscalableamyloidfibrilformationmethod
AT goumapelagiairene novelinexpensiveandscalableamyloidfibrilformationmethod