Polychlorinated Biphenyls Inhibit Amyloid Fibril Formation
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چکیده
منابع مشابه
Catechol derivatives inhibit the fibril formation of amyloid-beta peptides.
The inhibition of fibril formation of amyloid beta proteins (A beta) would be attractive therapeutic targets for the treatment of Alzheimer's disease (AD). Dopamine (DA) and other catechol derivatives were used as inhibitory factors for A beta fibril formation. The fibril formation of A beta was monitored by Thioflavin T fluorescence, a transmission electron microscopy (TEM) and a total interna...
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Light chain (or AL) amyloidosis is characterized by the pathological deposition of insoluble fibrils of immunoglobulin light chain fragments in various tissues, walls of blood vessels, and basement membranes. In the present investigation, the in vitro assembly of a recombinant amyloidogenic light chain variable domain, SMA, on various surfaces was monitored using atomic force microscopy. SMA fo...
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Polychlorinated biphenyls (PCBs) are industrial compounds with multiple industrial and commercial uses (Table 41.1). PCBs are chemically inert and stable when heated. These properties contribute greatly to PCBs having become environmental contaminants. The chemical inertness and heat stability properties that make PCBs desirable for industry also protect them from destruction when the products ...
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Using atomic force microscopy (AFM) we investigated the interaction of amyloid beta (Aβ) peptide with chemically modified surfaces in order to better understand the mechanism of amyloid toxicity, which involves interaction of amyloid with cell membrane surfaces. We compared the structure and density of Aβ fibrils on positively and negatively charged as well as hydrophobic chemically-modified su...
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The lack of understanding of amyloid fibril formation at the molecular level is a major obstacle in devising strategies to interfere with the pathologies linked to peptide or protein aggregation. In particular, little is known on the role of intermediates and fibril elongation pathways as well as their dependence on the intrinsic tendency of a polypeptide chain to self-assembly by beta-sheet fo...
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ژورنال
عنوان ژورنال: Chemistry & Biology
سال: 2004
ISSN: 1074-5521
DOI: 10.1016/j.chembiol.2004.11.016