Effect of lipids on the conformation of an antigenic determinant for experimental autoimmune neuritis.
The conformation of SP-26, the synthetic peptide (residues 53-78) of myelin P2 protein that causes experimental autoimmune neuritis (EAN) in the peripheral nervous system, has been studied in lipid environments and in water/trifluoroethanol (TFE) mixture using circular dichroism (CD) spectroscopy and Fourier transform infra-red (FTIR) spectroscopy. SP-26 becomes more structured on binding with micelles formed from anionic lipids and in the presence of TFE. On the other hand, zwitterionic lipids have a denaturing effect or no effect on the conformation of SP-26. The present results suggest that the disease-modulating effects of various lipids are closely related to their ability to induce conformational change in the antigenic region of P2 protein.
Shin
H C
HC
Protein Engineering Laboratory, Hanhyo Institute of Technology, Taejon, Korea. hcshin@donald.hanhyo.co.kr
D002942:Circular Dichroism; D000939:Epitopes / Q000737:chemistry*; D008055:Lipids / Q000737:chemistry*; D008823:Micelles; D018996:Myelin P2 Protein / Q000737:chemistry* / Q000276:immunology; D010446:Peptide Fragments / Q000737:chemistry* / Q000276:immunology; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions; D017550:Spectroscopy, Fourier Transform Infrared; D014270:Trifluoroethanol / Q000737:chemistry
D000939:Epitopes; D008055:Lipids; D008823:Micelles; D018996:Myelin P2 Protein; D010446:Peptide Fragments; D012996:Solutions; D014270:Trifluoroethanol