Current time in Korea 07:48 May 15 (Sat) Year 2021 KCS KCS Publications
KCS Publications
My Journal  Log In  Register
HOME > Search > Browsing(BKCS) > Archives

Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 25, Number 6
BKCSDE 25(6)
June 20, 2004 

Molecular Dynamics Simulations on β Amyloid Peptide (25-35) in Aqueous Trifluoroethanol Solution
Sangwon Lee, Yangmee Kim*
A β25-35, Conformation, Hydrogen bond, TFE, MD simulation
Amyloid peptide (A β) is the major component of senile plaques found in the brain of patient of Alzheimer's disease. β-amyloid peptide (25-35) (A β25-35) is biologically active fragment of A β. The three-dimensional structure of A β25-35 in aqueous solution with 50% (vol/vol) TFE determined by NMR spectroscopy previously adopts an α-helical conformation from Ala30 to Met35. It has been proposed that A β(25-35) exhibits pH- and concentration-dependent α-helix↔ β-sheet transition. This conformational transition with concomitant peptide aggregation is a possible mechanism of plaque formation. Here, in order to gain more insight into the mechanism of α-helix formation of A β25-35 peptide by TFE, which particularly stabilizes α-helical conformation, we studied the secondary-structural elements of A β25-35 peptide by molecular dynamics simulations. Secondary structural elements determined from NMR spectroscopy in aqueous TFE solution are preserved during the MD simulation. TFE/water mixed solvent has reduced capacity for forming hydrogen bond to the peptide compared to pure water solvent. TFE allows A β25-35 to form bifurcated hydrogen bonds to TFE as well as to residues in peptide itself. MD simulation in this study supports the notion that TFE can act as an α-helical structure forming solvent.
838 - 842
Full Text