Pore Formation by Amyloid-like Peptides: Effects of the Nonpolar-Polar Sequence Pattern.

ABSTRACT: One of the mechanisms accounting for the toxicity of amyloid peptides in diseases like Alzheimer's and Parkinson's is the formation of pores on the plasma membrane of neurons. Here, we perform unbiased all-atom simulations of the full membrane damaging pathway, which includes adsorption, aggregation, and perforation of the lipid bilayer accounting for pore-like structures. Simulations are performed using four peptides made with the same amino acids. Differences in the nonpolar-polar sequence pattern of these peptides prompt them to adsorb into the membrane with the extended conformations oriented either parallel [peptide labeled F1, Ac-(FKFE)₂-NH₂], perpendicular (F4, Ac-FFFFKKEE-NH₂), or with an intermediate orientation (F2, Ac-FFKKFFEE-NH₂, and

SUBMITTER: Rangubpit W 

PROVIDER: S-EPMC11443323 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature