Conformation of β-Amyloid Peptide (25-35) in Trifluoroethanol/Water Solution = TFE수용액중에서의 β-Amuloid Peptide (25-35)의 구조 연구

다국어 초록 (Multilingual Abstract)

β Amyloid peptide(Aβ) is the major component of senile plaques found in the brain of patient of Alzheimer's disease. Aβ25-35 is biologically active fragment of Aβ. The three-dimensional structure of β amyloid peptide (25-35) in aqueous solution with 50% (vol/vol) 2,2,2-trifluoroethanol was determined by NMR spectroscopy and interaction between β amyloid peptide (25-35) and TFE/water solvent was investigated by molecular dynamics simulation. Aβ25-35 in 50% TFE/water solution adopts a helical conformation from Ala^30 to Met^35 and aromatic rings of hydrophobic side chains in the center of the helix protrude outside. In order to investigate the effects of TFE in protein folding, MD simulations on Aβ25-35 in 50% TFE/water solution were performed. According to the MD simulations, TFE increased the ability of Aβ25-35 to form bifurcated hydrogen bonding with solvent and itself to retain α-helical structure.