Chirality of Amyloid Suprastructures
作者： Noa Rubin , Emanuel Perugia , Michal Goldschmidt , Mati Fridkin , Lia Addadi
DOI: 10.1021/JA800328Y
关键词:
摘要: Amyloids are pathological fibrillar aggregates of proteins related to more than 20 different diseases. Amyloid fibers have a characteristic cross-β structure consisting series β-strands extended perpendicular the fiber axis and joined by hydrogen bonds parallel direction. Fibril aggregation results in helical suprastructures. Here we used high-resolution SEM cryo-SEM for study chirality amyloid suprastructure. We found that amyloids Aβ1-40 hen lysozyme form at all hierarchical levels always only left-handed helices. In contrast, formed N-terminal sequence serum A (SAA1-12) consist right-handed helices exclusively. Consistently, peptide enantiomer, (R)-aminoacids, exclusively conclude opposite handedness SAA1-12 is an intrinsic feature structure. The observed suprastr...
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