Key result
Internal disulfide cyclization of peptide A15 produced analogs that were recognized one to two orders of magnitude better than linear A15 in ELISA and biosensor experiments.
Effect estimate: one to two orders of magnitude better
Internal disulfide cyclization of viral antigenic peptides stabilizes a bioactive-like structure, significantly improving antigenicity compared to linear peptides.
May enhance viral peptide antigenicity; leaves open translation to human vaccines or diagnostics.
Antigenic site A of foot-and-mouth disease virus (serotype C) has been reproduced by means of cyclic versions of peptide A15, YTASARGDLAHLTTT, corresponding to residues 136-150 of envelope protein VP1. A structural basis for the design of the cyclic peptides is provided by crystallographic data from complexes between the Fab fragments of anti-site A monoclonal antibodies and A15, in which the bound peptide is folded into a quasi-cyclic pattern. Head-to-tail cyclizations of A15 do not provide peptides of superior antigenicity. Internal disulfide cyclization, however, leads to analogs which are recognized as one to two orders of magnitude better than linear A15 in both ELISA and biosensor experiments. CD and NMR studies show that the best antigen, CTASARGDLAHLTT-Ahx-C (disulfide), is very insensitive to environment-induced conformational change, suggesting that cyclization helps to stabilize a bioactive-like structure.
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Valero et al. (2000) studied Foot-and-mouth disease virus. Internal disulfide cyclization of peptide A15 vs. Linear A15 peptide was evaluated on Antigenicity (recognition in ELISA and biosensor experiments) (one to two orders of magnitude better). Internal disulfide cyclization of peptide A15 produced analogs that were recognized one to two orders of magnitude better than linear A15 in ELISA and biosensor experiments.
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