title: Fibrillogenesis in ADan peptides is inhibited by biphenyl ethers.
abstract: In this study, biphenyl ethers of diverse functionality were used to assess their effect on fibrillogenesis of both the oxidized and reduced ADan peptides, in vitro. It was noted that these compounds not only stalled fibrillogenesis but were also able to disrupt pre-formed fibers. The EC(50) values for the inhibition of this process lie in the nanomolar range for 50 microM of peptide concentration, indicating the high potency of these compounds as inhibitors. It was found that these compounds impart to the peptides, an alpha-helical conformation which does not allow them to aggregate and form fibrils. These studies also point out that the transition of peptides through alpha-helical conformation may be a prelude to the onset of fibrillogenesis for oxADan peptides.
authors.affiliation: Department of Biochemistry, South Campus, University of Delhi, New Delhi 110021, India.
authors.forename: Ira
authors.initials: I
authors.lastname: Surolia
authors.forename: Manmohan
authors.initials: M
authors.lastname: Chhibber
authors.forename: Debi Prasad
authors.initials: DP
authors.lastname: Sarkar
authors.forename: Sharmistha
authors.initials: S
authors.lastname: Sinha
mesh_terms: D000682:Amyloid / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D001713:Biphenyl Compounds / Q000737:chemistry*; D002942:Circular Dichroism; D003704:Dementia / Q000378:metabolism; D004987:Ethers / Q000737:chemistry*; D006801:Humans; D046529:Microscopy, Electron, Transmission; D010455:Peptides / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D001713:Biphenyl Compounds; D004987:Ethers; D010455:Peptides