Epitopic peptides representing the C-terminal (HA1) region of cleaved hemagglutinin of influenza virus from different serotypes were synthesized. Circular dichroism and Fourier-transform infrared spectroscopic data showed that peptides HS2 and HS3 have a predominantly α-helical conformation in trifluoroethanol. Recently a component band appearing between 1640 and 1635 cm-1 in the amide I region of the Fourier-transform infrared spectra of polypeptides has been correlated with strongly H-bonded β-turns (Ref. 8). Using this assignment, HS1 was found to contain less α-helix but have tendency to adopt β-turn(s). Interestingly, fragment HS2 with the highest α-helix content proved to be the poorest T-cell epitope among serotypes HS1-HS3.
|Number of pages||8|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - Jun 30 1993|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology