Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones

Misfolding of proteins is the basis of several proteinopathies. Chemical and pharmacological chaperones are small molecules capable of inducing the correct conformation of proteins, thus being of interest for human therapeutics. The most recent developments in medicinal chemistry and in the drug dev...

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Detalles Bibliográficos
Autores principales: Pereira, David M., Valentão, Patrícia, Andrade, Paula B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2018
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5896381/
https://www.ncbi.nlm.nih.gov/pubmed/29719681
http://dx.doi.org/10.1039/c7sc04712f
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author Pereira, David M.
Valentão, Patrícia
Andrade, Paula B.
author_facet Pereira, David M.
Valentão, Patrícia
Andrade, Paula B.
author_sort Pereira, David M.
collection PubMed
description Misfolding of proteins is the basis of several proteinopathies. Chemical and pharmacological chaperones are small molecules capable of inducing the correct conformation of proteins, thus being of interest for human therapeutics. The most recent developments in medicinal chemistry and in the drug development of pharmacological chaperones are discussed, with focus on lysosomal storage diseases.
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spelling pubmed-58963812018-05-01 Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones Pereira, David M. Valentão, Patrícia Andrade, Paula B. Chem Sci Chemistry Misfolding of proteins is the basis of several proteinopathies. Chemical and pharmacological chaperones are small molecules capable of inducing the correct conformation of proteins, thus being of interest for human therapeutics. The most recent developments in medicinal chemistry and in the drug development of pharmacological chaperones are discussed, with focus on lysosomal storage diseases. Royal Society of Chemistry 2018-01-10 /pmc/articles/PMC5896381/ /pubmed/29719681 http://dx.doi.org/10.1039/c7sc04712f Text en This journal is © The Royal Society of Chemistry 2018 http://creativecommons.org/licenses/by-nc/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported Licence (CC BY-NC 3.0)
spellingShingle Chemistry
Pereira, David M.
Valentão, Patrícia
Andrade, Paula B.
Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones
title Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones
title_full Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones
title_fullStr Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones
title_full_unstemmed Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones
title_short Tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones
title_sort tuning protein folding in lysosomal storage diseases: the chemistry behind pharmacological chaperones
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5896381/
https://www.ncbi.nlm.nih.gov/pubmed/29719681
http://dx.doi.org/10.1039/c7sc04712f
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