Autori: Li, C.; Orbulescu, J.; Sui, G.; Leblanc, R. M.

Editorial: David G. Whitten, ACS, Langmuir, 20 (20), p.8641-8645, 2004.

Rezumat:

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

URL: http://pubs.acs.org/cgi-bin/article.cgi/langd5/2004/20/i20/pdf/la0490339.pdf