Comparison of the structures of beta amyloid peptide (25-35) and substance P in trifluoroethanol/water solution.
The three-dimensional structure of beta amyloid peptide (25-35) in aqueous solution with 50% (vol/vol) 2,2,2-trifluoroethanol was determined by NMR spectroscopy. Beta amyloid peptide(Abeta) is the major component of senile plaques found in the brain of patient of Alzheimer's disease. Abeta25-35 is biologically active fragment of Abeta and exhibits some sequence homology with the tachykinin family. In this study, we present the structural similarity between Abeta25-35 and substance P which is a member of tachykinin family in order to examine the possibility of sharing pathways mediated by tachykinin receptors. Both peptides have alpha-helical structures in their C-terminal regions and aromatic rings or hydrophobic side chains in the center of the helix protrude outside. These conformational features are expected to be the key for the interaction with the receptors.
Lee
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Department of Chemistry, Konkuk University, Seoul, Korea.
Suh
Y H
YH
Kim
S
S
Kim
Y
Y
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D002942:Circular Dichroism; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013373:Substance P / Q000737:chemistry*; D014270:Trifluoroethanol / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C113041:amyloid beta-protein (35-25); D014867:Water; D013373:Substance P; D014270:Trifluoroethanol