Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides

Under certain conditions, many proteins/peptides are capable of self-assembly into various supramolecular formations: fibrils, films, amyloid gels. Such formations can be associated with pathological phenomena, for example, with various neurodegenerative diseases in humans (Alzheimer’s, Parkinson’s...

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Autores principales:	Oxana V. Galzitskaya, Olga M. Selivanova, Elena Y. Gorbunova, Leila G. Mustaeva, Viacheslav N. Azev, Alexey K. Surin
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	Aβ peptide amyloid fibril biofilm oligomer amyloidogenic regions Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/327c679fd13742118490747319b91ae9
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spelling	oai:doaj.org-article:327c679fd13742118490747319b91ae92021-11-25T18:32:41ZMechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides10.3390/nano111131292079-4991https://doaj.org/article/327c679fd13742118490747319b91ae92021-11-01T00:00:00Zhttps://www.mdpi.com/2079-4991/11/11/3129https://doaj.org/toc/2079-4991Under certain conditions, many proteins/peptides are capable of self-assembly into various supramolecular formations: fibrils, films, amyloid gels. Such formations can be associated with pathological phenomena, for example, with various neurodegenerative diseases in humans (Alzheimer’s, Parkinson’s and others), or perform various functions in the body, both in humans and in representatives of other domains of life. Recently, more and more data have appeared confirming the ability of many known and, probably, not yet studied proteins/peptides, to self-assemble into quaternary structures. Fibrils, biofilms and amyloid gels are promising objects for the developing field of research of nanobiotechnology. To develop methods for obtaining nanobiomaterials with desired properties, it is necessary to study the mechanism of such structure formation, as well as the influence of various factors on this process. In this work, we present the results of a study of the structure of biogels formed by four 10-membered amyloidogenic peptides: the VDSWNVLVAG peptide (AspNB) and its analogue VESWNVLVAG (GluNB), which are amyloidogenic fragments of the glucantransferase Bgl2p protein from a yeast cell wall, and amyloidogenic peptides Aβ(31–40), Aβ(33–42) from the Aβ(1–42) peptide. Based on the analysis of the data, we propose a possible mechanism for the formation of amyloid gels with these peptides.Oxana V. GalzitskayaOlga M. SelivanovaElena Y. GorbunovaLeila G. MustaevaViacheslav N. AzevAlexey K. SurinMDPI AGarticleAβ peptideamyloid fibrilbiofilmoligomeramyloidogenic regionsChemistryQD1-999ENNanomaterials, Vol 11, Iss 3129, p 3129 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Aβ peptide amyloid fibril biofilm oligomer amyloidogenic regions Chemistry QD1-999
spellingShingle	Aβ peptide amyloid fibril biofilm oligomer amyloidogenic regions Chemistry QD1-999 Oxana V. Galzitskaya Olga M. Selivanova Elena Y. Gorbunova Leila G. Mustaeva Viacheslav N. Azev Alexey K. Surin Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides
description	Under certain conditions, many proteins/peptides are capable of self-assembly into various supramolecular formations: fibrils, films, amyloid gels. Such formations can be associated with pathological phenomena, for example, with various neurodegenerative diseases in humans (Alzheimer’s, Parkinson’s and others), or perform various functions in the body, both in humans and in representatives of other domains of life. Recently, more and more data have appeared confirming the ability of many known and, probably, not yet studied proteins/peptides, to self-assemble into quaternary structures. Fibrils, biofilms and amyloid gels are promising objects for the developing field of research of nanobiotechnology. To develop methods for obtaining nanobiomaterials with desired properties, it is necessary to study the mechanism of such structure formation, as well as the influence of various factors on this process. In this work, we present the results of a study of the structure of biogels formed by four 10-membered amyloidogenic peptides: the VDSWNVLVAG peptide (AspNB) and its analogue VESWNVLVAG (GluNB), which are amyloidogenic fragments of the glucantransferase Bgl2p protein from a yeast cell wall, and amyloidogenic peptides Aβ(31–40), Aβ(33–42) from the Aβ(1–42) peptide. Based on the analysis of the data, we propose a possible mechanism for the formation of amyloid gels with these peptides.
format	article
author	Oxana V. Galzitskaya Olga M. Selivanova Elena Y. Gorbunova Leila G. Mustaeva Viacheslav N. Azev Alexey K. Surin
author_facet	Oxana V. Galzitskaya Olga M. Selivanova Elena Y. Gorbunova Leila G. Mustaeva Viacheslav N. Azev Alexey K. Surin
author_sort	Oxana V. Galzitskaya
title	Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides
title_short	Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides
title_full	Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides
title_fullStr	Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides
title_full_unstemmed	Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides
title_sort	mechanism of amyloid gel formation by several short amyloidogenic peptides
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/327c679fd13742118490747319b91ae9
work_keys_str_mv	AT oxanavgalzitskaya mechanismofamyloidgelformationbyseveralshortamyloidogenicpeptides AT olgamselivanova mechanismofamyloidgelformationbyseveralshortamyloidogenicpeptides AT elenaygorbunova mechanismofamyloidgelformationbyseveralshortamyloidogenicpeptides AT leilagmustaeva mechanismofamyloidgelformationbyseveralshortamyloidogenicpeptides AT viacheslavnazev mechanismofamyloidgelformationbyseveralshortamyloidogenicpeptides AT alexeyksurin mechanismofamyloidgelformationbyseveralshortamyloidogenicpeptides
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Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides

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