title: Amyloid-like formation by self-assembly of peptidolipids in two dimensions.
abstract: The accumulation of beta-amyloid peptide (Abeta) in the human brain is known to be the major cause that drives Alzheimer's disease pathogenesis. Abeta, a 39-42 amino acid peptide, is the cleavage product of amyloid precursor 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 Abeta 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.
authors.affiliation: Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33124, USA.
authors.forename: Changqing
authors.initials: C
authors.lastname: Li
authors.forename: Jhony
authors.initials: J
authors.lastname: Orbulescu
authors.forename: Guodong
authors.initials: G
authors.lastname: Sui
authors.forename: Roger M
authors.initials: RM
authors.lastname: Leblanc
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D000682:Amyloid / Q000138:chemical synthesis* / Q000737:chemistry; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D000686:Amyloidosis / Q000378:metabolism; D008055:Lipids / Q000737:chemistry*; D008954:Models, Biological; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D013499:Surface Properties
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D008055:Lipids; D010446:Peptide Fragments; C113042:amyloid beta-protein (31-35)