作者: Pin-Nan Cheng , Cong Liu , Minglei Zhao , David Eisenberg , James S. Nowick
DOI: 10.1038/NCHEM.1433
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摘要: The amyloid protein aggregation associated with diseases such as Alzheimer's, Parkinson's and type II diabetes (among many others) features a bewildering variety of β-sheet-rich structures in transition from native proteins to ordered oligomers fibres. variation the amino-acid sequences β-structures presents challenge developing model system β-sheets for study various aggregates. Here, we introduce family robust β-sheet macrocycles that can serve platform display heptapeptide different proteins. We have tailored these mimics (ABSMs) antagonize proteins, thereby reducing toxicity describe inhibitory properties ABSMs containing amyloidogenic peptides amyloid-β peptide Alzheimer's disease, β(2)-microglobulin dialysis-related amyloidosis, α-synuclein islet polypeptide diabetes, human yeast prion Tau, which forms neurofibrillary tangles.