Structural comparison between retro-inverso and parent peptides: Molecular basis for the biological activity of a retro-inverso analogue of the immunodominant fragment of VP1 coat protein from foot-and-mouth disease virus
✍ Scribed by John A. Carver; Gennaro Esposito; Paolo Viglino; Federico Fogolari; Gilles Guichard; Jean-Paul Briand; Marc H. V. Van Regenmortel; Fred Brown; Paolo Mascagni
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1997
- Tongue
- English
- Weight
- 576 KB
- Volume
- 41
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Antibodies induced against intact foot-and-mouth disease Virus (FMDV) particles bind to the retro-inverso analogue of fragment 141-159 of the viral coat protein VP1 of FMDV, variant A, equally well as to the parent peptide. A conformational investigation of this retro-inverso peptide was carried out by nmr spectroscopy and restrained molecular modeling in order to identify the structural basis for the antigenic mimicry between these retro-inverso and parent peptides. In 100% trifluoroethanol a well-defined left-handed a-helical region exists from residue 150 to residue 159, which is consistently present in all conformational families