Modeling Oligomeric Structures of Amyloid forming Peptides

Division Of Basic Sciences - Nci

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Abstract

In this period we published two papers. In the first we proposed a range of concentric beta-barrel models and compare their dimensions to image-averaged electron micrographs of Beta-Amyloid42. The smaller oligomers have 6, 8, 12, 16, and 18 monomers. These beads string together to form necklace-like beaded-annular-protofibrils (bAPFs). These gradually morph into smooth-APFs in which a S3 beta-barrel is shielded on one or both sides by beta-barrels formed from S1 and S2 segments. In the second we extend our beta-amyloid peptide models of oligomers, annular protofibrils, tubular protofibrils, lipoproteins, and ion channels to the alpha, beta and gamma synuclein family which has been implicated in Parkinson's Disease.