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  • Title: The formation of a novel supramolecular structure by amyloid of poly-L-glutamic acid.
    Author: Bai F, Zeng C, Yang S, Zhang Y, He Y, Jin J.
    Journal: Biochem Biophys Res Commun; 2008 May 09; 369(3):830-4. PubMed ID: 18307983.
    Abstract:
    Polyglutamic acid (PE) has been shown to form amyloid fibrils in vitro under pH value of 4.0. However, under the pH of 2.0, a further self-association process resulting in a novel supramolecular structure was observed. These supramolecular assemblies had diameters ranging from 1 to 20 microm and lengths up to several hundred microns, which were significantly larger than those of typical "amyloid fibrils". The existence of amyloid-like structure within these assemblies was confirmed with Fourier transform infrared spectroscopy and Thioflavin T fluorescence assay. The aggregation process of PE was studied by direct observation of electronic microscopy. The supramolecular assemblies appeared to be formed in a hierarchical process in which the preformed amyloid-like subunits self-assembled into higher-order assemblies in a well-organized pattern.
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