Circular dichroism and Fourier-transform infrared spectroscopic studies on T-cell epitopic peptide fragments of influenza virus hemagglutinin.
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 alpha-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 beta-turns (Ref. 8). Using this assignment, HS1 was found to contain less alpha-helix but have tendency to adopt beta-turn(s). Interestingly, fragment HS2 with the highest alpha-helix content proved to be the poorest T-cell epitope among serotypes HS1-HS3.
Holly
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S
Central Research Institute of Chemistry, Budapest, Hungary.
Majer
Z
Z
Tóth
G K
GK
Váradi
G
G
Rajnavölgyi
E
E
Laczkó
I
I
Hollósi
M
M
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D000939:Epitopes / Q000737:chemistry*; D005583:Fourier Analysis; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000737:chemistry* / Q000276:immunology; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D016339:Spectrometry, Mass, Fast Atom Bombardment; D013055:Spectrophotometry, Infrared / Q000379:methods; D013601:T-Lymphocytes / Q000276:immunology*; D014759:Viral Envelope Proteins / Q000737:chemistry
D000939:Epitopes; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D010446:Peptide Fragments; D014759:Viral Envelope Proteins