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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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Detalles Bibliográficos
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
Descripción
Sumario:[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.