Circular dichroism and Fourier-transform infrared spectroscopic studies on T-cell epitopic peptide fragments of influenza virus hemagglutinin.

Abstract:

: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.

authors

Holly S,Majer Z,Tóth GK,Váradi G,Rajnavölgyi E,Laczkó I,Hollósi M

doi

10.1006/bbrc.1993.1759

subject

Has Abstract

pub_date

1993-06-30 00:00:00

pages

1247-54

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71759-6

journal_volume

193

pub_type

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