Sup35NMp Morphology Evaluation on Au, Si, Formvar and Mica Surfaces Using AFM, SEM and TEM

Research output

3 Citations (Scopus)

Abstract

Prion and some other incurable human neurodegenerative diseases are associated with misfolding of specific proteins, followed by the formation of amyloids. Despite the widespread usage of the transmission electron and of the atomic force microscopy for studing such amyloids, many related methodological issues still have not been studied until now. Here, we consider one of the first amyloids found in Saccharomyces cerevisiae yeast, i.e. Sup35NMp, to study the adsorption of monomeric protein and its fibrils on the surface of mica, silica, gold and on formvar film. Comparison of linear characteristics of these units calculated by processing of images obtained by the atomic force, transmission and scanning electron microscopy was carried out. The minimal number of measurements of fibril diameters to obtain the values in a given confidence interval were determined. We investigated the film formed by monomeric protein on mica surface, which veiled some morphology features of fibrils. Besides, we revealed that parts of the Sup35NMp excluded from the fibril core can form a wide “coat”. The length of the protein forming the core of the fibrils was estimated.
Original languageEnglish
Pages (from-to)5-14
Number of pages10
JournalJournal of Structural Biology
Volume201
Issue number1
Early online date31 Oct 2017
DOIs
Publication statusPublished - Jan 2018

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Amyloid
Proteins
Scanning Transmission Electron Microscopy
Atomic Force Microscopy
Prions
Silicon Dioxide
Gold
Neurodegenerative Diseases
Adsorption
Saccharomyces cerevisiae
Yeasts
Electrons
Confidence Intervals
mica
polyvinyl acetate

Scopus subject areas

  • Structural Biology

Cite this

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title = "Sup35NMp Morphology Evaluation on Au, Si, Formvar and Mica Surfaces Using AFM, SEM and TEM",
abstract = "Prion and some other incurable human neurodegenerative diseases are associated with misfolding of specific proteins, followed by the formation of amyloids. Despite the widespread usage of the transmission electron and of the atomic force microscopy for studing such amyloids, many related methodological issues still have not been studied until now. Here, we consider one of the first amyloids found in Saccharomyces cerevisiae yeast, i.e. Sup35NMp, to study the adsorption of monomeric protein and its fibrils on the surface of mica, silica, gold and on formvar film. Comparison of linear characteristics of these units calculated by processing of images obtained by the atomic force, transmission and scanning electron microscopy was carried out. The minimal number of measurements of fibril diameters to obtain the values in a given confidence interval were determined. We investigated the film formed by monomeric protein on mica surface, which veiled some morphology features of fibrils. Besides, we revealed that parts of the Sup35NMp excluded from the fibril core can form a wide “coat”. The length of the protein forming the core of the fibrils was estimated.",
keywords = "Amyloid, Fibril, Microscopy, Prion, Structure, Yeasts, AMYLOID FIBERS, DOMAIN, DETERMINANT, YEAST SUP35, SACCHAROMYCES-CEREVISIAE, SYNUCLEIN STRAINS, ATOMIC-FORCE MICROSCOPY, PRION VARIANTS, BETA-SHEET STRUCTURE, DIVERSITY",
author = "Sokolov, {P. A.} and Bondarev, {S. A.} and Belousov, {M. V.} and Zhouravleva, {G. A.} and N.A. Kasyanenko",
year = "2018",
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T1 - Sup35NMp Morphology Evaluation on Au, Si, Formvar and Mica Surfaces Using AFM, SEM and TEM

AU - Sokolov, P. A.

AU - Bondarev, S. A.

AU - Belousov, M. V.

AU - Zhouravleva, G. A.

AU - Kasyanenko, N.A.

PY - 2018/1

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N2 - Prion and some other incurable human neurodegenerative diseases are associated with misfolding of specific proteins, followed by the formation of amyloids. Despite the widespread usage of the transmission electron and of the atomic force microscopy for studing such amyloids, many related methodological issues still have not been studied until now. Here, we consider one of the first amyloids found in Saccharomyces cerevisiae yeast, i.e. Sup35NMp, to study the adsorption of monomeric protein and its fibrils on the surface of mica, silica, gold and on formvar film. Comparison of linear characteristics of these units calculated by processing of images obtained by the atomic force, transmission and scanning electron microscopy was carried out. The minimal number of measurements of fibril diameters to obtain the values in a given confidence interval were determined. We investigated the film formed by monomeric protein on mica surface, which veiled some morphology features of fibrils. Besides, we revealed that parts of the Sup35NMp excluded from the fibril core can form a wide “coat”. The length of the protein forming the core of the fibrils was estimated.

AB - Prion and some other incurable human neurodegenerative diseases are associated with misfolding of specific proteins, followed by the formation of amyloids. Despite the widespread usage of the transmission electron and of the atomic force microscopy for studing such amyloids, many related methodological issues still have not been studied until now. Here, we consider one of the first amyloids found in Saccharomyces cerevisiae yeast, i.e. Sup35NMp, to study the adsorption of monomeric protein and its fibrils on the surface of mica, silica, gold and on formvar film. Comparison of linear characteristics of these units calculated by processing of images obtained by the atomic force, transmission and scanning electron microscopy was carried out. The minimal number of measurements of fibril diameters to obtain the values in a given confidence interval were determined. We investigated the film formed by monomeric protein on mica surface, which veiled some morphology features of fibrils. Besides, we revealed that parts of the Sup35NMp excluded from the fibril core can form a wide “coat”. The length of the protein forming the core of the fibrils was estimated.

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KW - Microscopy

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KW - Structure

KW - Yeasts

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KW - DETERMINANT

KW - YEAST SUP35

KW - SACCHAROMYCES-CEREVISIAE

KW - SYNUCLEIN STRAINS

KW - ATOMIC-FORCE MICROSCOPY

KW - PRION VARIANTS

KW - BETA-SHEET STRUCTURE

KW - DIVERSITY

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