Design, characterization, and use of a novel amyloid β-protein control for assembly, neurotoxicity, and gene expression studies

ABSTRACT: A key pathogenic agent in Alzheimer’s disease (AD) is the amyloid β-protein (Aβ), which self-assembles into a variety of neurotoxic structures. Establishing structure-activity relationships for these assemblies is critical for proper therapeutic target identification and design. We examined the effects of Aβ monomers, dimers, higher-order oligomers, and fibrils on gene expression in primary rat hippocampal neurons. As opposed to “reverse” Aβ or non-Aβ peptides typically used as controls in such studies, we designed novel scrambled Aβ peptides predicted to behave distinctly from native Aβ. Significant changes in gene expression were observed for all peptide assemblies, but fibrils induced the largest changes. Significant changes in gene expression were observed for all peptide

ORGANISM(S): Rattus norvegicus

SUBMITTER: Giovanni Coppola 

PROVIDER: E-GEOD-85952 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress