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Analysis of Protein Conformational Strains—A Key for New Diagnostic Methods of Human Diseases

α-Synuclein is a naturally unfolded protein which easily aggregates and forms toxic inclusions and deposits. It is associated with several neurodegenerative diseases, including Parkinson’s disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA). These diseases, called synucl...

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Detalles Bibliográficos
Autor principal: Surguchov, Andrei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7215537/
https://www.ncbi.nlm.nih.gov/pubmed/32316500
http://dx.doi.org/10.3390/ijms21082801
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author Surguchov, Andrei
author_facet Surguchov, Andrei
author_sort Surguchov, Andrei
collection PubMed
description α-Synuclein is a naturally unfolded protein which easily aggregates and forms toxic inclusions and deposits. It is associated with several neurodegenerative diseases, including Parkinson’s disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA). These diseases, called synucleinopathies, have overlapping symptoms but require different methods of treatment. There are no reliable approaches for early diagnoses of these diseases, and as a result, the treatment begins late, and the disorders are often misdiagnosed. Recent studies revealed that α-synuclein forms distinctive spatial structures or strains at the early steps of these diseases, which may be used for early diagnosis. One of these early diagnostic methods called PMCA (protein misfolding cyclic amplification) allows identification of the distinct α-synuclein strains specific for different human diseases. The method is successfully used for differential diagnosis of patients with PD and MSA.
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spelling pubmed-72155372020-05-22 Analysis of Protein Conformational Strains—A Key for New Diagnostic Methods of Human Diseases Surguchov, Andrei Int J Mol Sci Communication α-Synuclein is a naturally unfolded protein which easily aggregates and forms toxic inclusions and deposits. It is associated with several neurodegenerative diseases, including Parkinson’s disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA). These diseases, called synucleinopathies, have overlapping symptoms but require different methods of treatment. There are no reliable approaches for early diagnoses of these diseases, and as a result, the treatment begins late, and the disorders are often misdiagnosed. Recent studies revealed that α-synuclein forms distinctive spatial structures or strains at the early steps of these diseases, which may be used for early diagnosis. One of these early diagnostic methods called PMCA (protein misfolding cyclic amplification) allows identification of the distinct α-synuclein strains specific for different human diseases. The method is successfully used for differential diagnosis of patients with PD and MSA. MDPI 2020-04-17 /pmc/articles/PMC7215537/ /pubmed/32316500 http://dx.doi.org/10.3390/ijms21082801 Text en © 2020 by the author. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Surguchov, Andrei
Analysis of Protein Conformational Strains—A Key for New Diagnostic Methods of Human Diseases
title Analysis of Protein Conformational Strains—A Key for New Diagnostic Methods of Human Diseases
title_full Analysis of Protein Conformational Strains—A Key for New Diagnostic Methods of Human Diseases
title_fullStr Analysis of Protein Conformational Strains—A Key for New Diagnostic Methods of Human Diseases
title_full_unstemmed Analysis of Protein Conformational Strains—A Key for New Diagnostic Methods of Human Diseases
title_short Analysis of Protein Conformational Strains—A Key for New Diagnostic Methods of Human Diseases
title_sort analysis of protein conformational strains—a key for new diagnostic methods of human diseases
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7215537/
https://www.ncbi.nlm.nih.gov/pubmed/32316500
http://dx.doi.org/10.3390/ijms21082801
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