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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2015
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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. |
format | Online Article Text |
id | pubmed-4941208 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
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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