title: Supramolecular Glycosylation Accelerates Proteolytic Degradation of Peptide Nanofibrils.
abstract: 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.
authors.affiliation: Department of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Dan
authors.initials: D
authors.lastname: Yuan
authors.affiliation: Department of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Junfeng
authors.initials: J
authors.lastname: Shi
authors.affiliation: Department of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Xuewen
authors.initials: X
authors.lastname: Du
authors.affiliation: Department of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Ning
authors.initials: N
authors.lastname: Zhou
authors.affiliation: Department of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.
authors.forename: Bing
authors.initials: B
authors.lastname: Xu
mesh_terms: D020816:Amino Acid Motifs; D002151:Calorimetry / Q000379:methods; D000939:Epitopes / Q000737:chemistry; D006001:Glycoconjugates / Q000737:chemistry / Q000378:metabolism; D006031:Glycosylation; D020100:Hydrogels / Q000737:chemistry; D046529:Microscopy, Electron, Transmission; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D059748:Proteolysis; D060327:Solid-Phase Synthesis Techniques
chemical_list: D000939:Epitopes; D006001:Glycoconjugates; D020100:Hydrogels; D010455:Peptides