Heterologous stacking of prion protein peptides reveals structural details of fibrils and facilitates complete inhibition of fibril growth.

ABSTRACT: Fibrils play an important role in the pathogenesis of amyloidosis; however, the underlying mechanisms of the growth process and the structural details of fibrils are poorly understood. Crucial in the fibril formation of prion proteins is the stacking of PrP monomers. We previously proposed that the structure of the prion protein fibril may be similar as a parallel left-handed beta-helix. The beta-helix is composed of spiraling rungs of parallel beta-strands, and in the PrP model residues 105-143 of each PrP monomer can contribute two beta-helical rungs to the growing fibril. Here we report data to support this model. We show that two cyclized human PrP peptides corresponding to residues 105-124 and 125-143, based on two single rungs of the left-handed beta-helical core of the human PrP(Sc)

SUBMITTER: Boshuizen RS 

PROVIDER: S-EPMC2676011 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature