rottlerin and baicalein

Many amyloid inhibitors resemble molecules that form chemical aggregates, which are known to inhibit many proteins. Eight known chemical aggregators inhibited amyloid formation of the yeast and mouse prion proteins Sup35 and recMoPrP in a manner characteristic of colloidal inhibition. Similarly, three known anti-amyloid molecules inhibited beta-lactamase in a detergent-dependent manner, which suggests that they too form colloidal aggregates. The colloids localized to preformed fibers and prevented new fiber formation in electron micrographs. They also blocked infection of yeast cells with Sup35 prions, which suggests that colloidal inhibition may be relevant in more biological milieus.

Topics: Acetophenones; Animals; Benzopyrans; beta-Lactamase Inhibitors; beta-Lactamases; Clioquinol; Congo Red; Detergents; Flavanones; Mice; Microscopy, Electron, Transmission; Molecular Structure; Molecular Weight; Particle Size; Peptide Termination Factors; Phenolphthaleins; Phthalimides; Prions; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sensitivity and Specificity; Structure-Activity Relationship

Topics: Acetophenones; Amyloid; Amyloid beta-Peptides; Artifacts; Benzopyrans; Congo Red; Drug Evaluation, Preclinical; Flavanones; Microscopy, Electron, Transmission; Molecular Structure; Molecular Weight; Particle Size; Phenolphthaleins; Phthalimides; Sensitivity and Specificity; Structure-Activity Relationship