Abstract
A tridecapeptide with the sequence CCEICCNPACFGC has been synthesized to reproduce the active moiety of a heat stable enterotoxin from Vibrio cholerae. The proton NMR analysis indicates, for the active synthetic fragment, a rigid secondary structure stabilised by three disulfide bridges. Such a rigid peptide, suitably detoxified and activated, could be a good candidate to be used as a carrier for linear bioactive peptides or other functional groups.
| Original language | English |
|---|---|
| Pages (from-to) | 1053-1059 |
| Number of pages | 7 |
| Journal | Journal of Biomolecular Structure and Dynamics |
| Volume | 16 |
| Issue number | 5 |
| Publication status | Published - 1999 |
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ASJC Scopus subject areas
- Molecular Biology
- Structural Biology
Cite this
Di Maro, D., Scarselli, M., Bernini, A., Cresti, S., Rossolini, G. M., Lozzi, L., Neri, P., & Niccolai, N. (1999). On the structural stability of a small bioactive peptide of potential use in biotechnology. Journal of Biomolecular Structure and Dynamics, 16(5), 1053-1059.