Abstract
The neuritic plaques formed by amyloid β-peptide (Aβ) play a seminal role in the pathogenesis of Alzheimer's disease (AD). Aβ sequence 25−35 (GSNKGAIIGLM) is among the most frequently studied Aβ derivatives for the reason that it possesses the structural characteristic of Aβ and remains neurotoxic. Aβ(25−35) was modified with an aliphatic chain (C18) at the N-terminal of the peptide for the study of the Langmuir monolayer at the air−water interface. The main advantage of the 2D approach is the self-assembly of the peptide moiety in the subphase, and therefore the aggregation process of the peptidolipid Aβ(25−35) was monitored by surface pressure and surface potential−area isotherms. The real-time epifluorescence microscopy was utilized to observe the topography of the domains formed, whereas polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) provided the information on the structural features of the domains at the air−water interface. Langmuir−Blodgett films were prepared to examine by circular dichroism (CD) the conformation of the peptidolipid film in the domains.
