Rationally designed peptoids modulate aggregation of amyloid-beta 40.

ACS chemical neuroscience (2014-04-03)
J Phillip Turner, Tammy Lutz-Rechtin, Kelly A Moore, Lauren Rogers, Omkar Bhave, Melissa A Moss, Shannon L Servoss
ABSTRACT

Alzheimer's disease (AD) is the most common form of dementia and the sixth leading cause of death in the United States. Plaques composed of aggregated amyloid-beta protein (Aβ) accumulate between the neural cells in the brain and are associated with dementia and cellular death. Many strategies have been investigated to prevent Aβ self-assembly into disease-associated β-sheet amyloid aggregates; however, a promising therapeutic has not yet been identified. In this study, a peptoid-based mimic of the peptide KLVFF (residues 16-20 of Aβ) was tested for its ability to modulate Aβ aggregation. Peptoid JPT1 includes chiral, aromatic side chains to induce formation of a stable helical secondary structure that allows for greater interaction between the aromatic side chains and the cross β-sheet of Aβ. JPT1 was found to modulate Aβ40 aggregation, specifically decreasing lag time to β-sheet aggregate formation as well as the total number of fibrillar, β-sheet structured aggregates formed. These results suggest that peptoids may be able to limit the formation of Aβ aggregates that are associated with AD.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Piperidine, ReagentPlus®, 99%
Sigma-Aldrich
Piperidine, ≥99.5%, purified by redistillation
Sigma-Aldrich
N-Boc-1,4-butanediamine, ≥97.0% (GC/NT)
Sigma-Aldrich
Piperidine solution, suitable for peptide synthesis, 20% in DMF
Sigma-Aldrich
Piperidine, biotech. grade, ≥99.5%
Sigma-Aldrich
Piperidine, puriss. p.a., ≥99.0% (GC/T)

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