title: The post-translational incorporation of arginine into a beta-amyloid peptide increases the probability of alpha-helix formation.
abstract: The beta-amyloid peptide (beta AP1-40) inhibited the in vitro post-translational incorporation of [14C]arginine at the N-terminus of brain soluble proteins and was labelled by the incorporation of [14C]arginine. Addition of arginine at the N-terminal position of beta AP1-40 is predicted to increase the probability of an alpha-helix structure being formed on the first residues with a higher hydrophilic characteristic, increasing the possibility of these residues being exposed to the aqueous environment. Unmodified beta AP1-40 has a low alpha-helix content and a higher probability of beta-turn formation. Accumulation of beta AP1-40 in Alzheimer's disease may therefore be due to a reduced arginylation reaction and consequently to a decrease in its normal degradation by the ubiquitin pathway.
authors: Dpto. Química Biológica, Universidad Nacional de Córdoba, Argentina.
authors: G
authors: G
authors: Bongiovanni
authors: G D
authors: GD
authors: Fidelio
authors: H S
authors: HS
authors: Barra
authors: M E
authors: ME
authors: Hallak
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D001120:Arginine / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D011336:Probability; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); D001120:Arginine