Abstract
Negatively-charged phospholipid membrane does not affect the random coil conformation of a non-neurotoxic amyloid-beeta-peptide having a retro-sequence 35-25 (Abeta 35-25), whereas it changes the conformation of a neurotoxic normal-sequence peptide A beeta 25-35 from a random coil to a beeta-sheet-like structure under the same condition. The formation of the ordered structure seems to be closely related to the expression of neurotoxicity.
Keywords: AMYLOID PEPTIDE 35-25, AMYLOID PEPTIDE 25-35, amyloid peptide