Scopul nostru este sprijinirea şi promovarea cercetării ştiinţifice şi facilitarea comunicării între cercetătorii români din întreaga lume.
Autori: Li, C.; Orbulescu, J.; Sui, G.; Leblanc, R. M.
Editorial: David G. Whitten, ACS, Langmuir, 20 (20), p.8641-8645, 2004.
The accumulation of ß-amyloid peptide (Aß) in the human brain is known to be the major cause that drives Alzheimer’s disease pathogenesis. Aß, a 39-42 amino acid peptide, is the cleavage product of amyloid precusor protein in the hydrophobic transmembrane region. The present study employs a two-dimensional (2D) approach. Two synthetic peptidolipids, C18-IIGLM-OH and C18-IIGLM-NH2, are selected based on the fragment 31-35 of Aß which is recognized as one of the determining segments that induces formation of amyloid fibril plaques. The aliphatic hydrocarbon chain C18 is attached to the N-terminal of the fragment 31-35 to facilitate the 2D study at the air-water interface. The aggregation process is observed by two measurements: (1) surface pressure-area and surface dipole moment-area isotherms and (2) epifluorescence microscopy of the Langmuir films to investigate the topography of the amyloid-like formation.
Cuvinte cheie: langmuir film, amyloid-like structure, aggregation, epi-fluorescence