Scopul nostru este sprijinirea şi promovarea cercetării ştiinţifice şi facilitarea comunicării între cercetătorii români din întreaga lume.
Autori: Robert C. Triulzi, Changqing Li, David Naistat, Jhony Orbulescu, and Roger M. Leblanc
Editorial: Brigitte Barry, American Chemical Society, Journal of Physical Chemistry C, 111 (12), p.4661-4666, 2007.
The neuritic plaques formed by amyloid beta-peptide (Abeta) play a seminal role in the pathogenesis of Alzheimer’s disease (AD). Abeta sequence 25-35 (GSNKGAIIGLM) is among the most frequently studied Abeta derivatives for the reason that it possesses the structural characteristic of Abeta and remains neurotoxic. Abeta(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 Abeta(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.
Cuvinte cheie: amyloid aggregation, PM-IRRAS, Langmuir film