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Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils

[Image: see text] Despite the recent consensus that the oligomers of amyloid peptides or aberrant proteins are cytotoxic species, there is still a need for an effective way to eliminate the oligomers. Based on the fact that normal proteins are more glycosylated than pathogenic proteins, we show that...

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Autores principales: Yuan, Dan, Shi, Junfeng, Du, Xuewen, Zhou, Ning, Xu, Bing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2015
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4941208/
https://www.ncbi.nlm.nih.gov/pubmed/26237170
http://dx.doi.org/10.1021/jacs.5b05888
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author Yuan, Dan
Shi, Junfeng
Du, Xuewen
Zhou, Ning
Xu, Bing
author_facet Yuan, Dan
Shi, Junfeng
Du, Xuewen
Zhou, Ning
Xu, Bing
author_sort Yuan, Dan
collection PubMed
description [Image: see text] Despite the recent consensus that the oligomers of amyloid peptides or aberrant proteins are cytotoxic species, there is still a need for an effective way to eliminate the oligomers. Based on the fact that normal proteins are more glycosylated than pathogenic proteins, we show that a conjugate of nucleobase, peptide, and saccharide binds to peptides from molecular nanofibrils and accelerates the proteolytic degradation of the molecular nanofibrils. As the first example of the use of supramolecular glycosylation to dissociate molecular nanofibrils and to accelerate the degradation of peptide aggregates, this work illustrates a new method that ultimately may lead to an effective approach for degrading cytotoxic oligomers of peptides or aberrant proteins.
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spelling pubmed-49412082016-08-05 Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils Yuan, Dan Shi, Junfeng Du, Xuewen Zhou, Ning Xu, Bing J Am Chem Soc [Image: see text] Despite the recent consensus that the oligomers of amyloid peptides or aberrant proteins are cytotoxic species, there is still a need for an effective way to eliminate the oligomers. Based on the fact that normal proteins are more glycosylated than pathogenic proteins, we show that a conjugate of nucleobase, peptide, and saccharide binds to peptides from molecular nanofibrils and accelerates the proteolytic degradation of the molecular nanofibrils. As the first example of the use of supramolecular glycosylation to dissociate molecular nanofibrils and to accelerate the degradation of peptide aggregates, this work illustrates a new method that ultimately may lead to an effective approach for degrading cytotoxic oligomers of peptides or aberrant proteins. American Chemical Society 2015-08-03 2015-08-19 /pmc/articles/PMC4941208/ /pubmed/26237170 http://dx.doi.org/10.1021/jacs.5b05888 Text en Copyright © 2015 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Yuan, Dan
Shi, Junfeng
Du, Xuewen
Zhou, Ning
Xu, Bing
Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils
title Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils
title_full Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils
title_fullStr Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils
title_full_unstemmed Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils
title_short Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils
title_sort supramolecular glycosylation accelerates proteolytic degradation of peptide nanofibrils
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4941208/
https://www.ncbi.nlm.nih.gov/pubmed/26237170
http://dx.doi.org/10.1021/jacs.5b05888
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