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. © 1999 Taylor & Francis Group, LLC.
DI MARO, D., Scarselli, M., Bernini, A., Cresti, S., Rossolini, G.M., Lozzi, L., et al. (1999). On the structural stability of a small bioactive peptide of potential unse in Biotechnology. JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 16(5), 1053-1059 [10.1080/07391102.1999.10508314].
On the structural stability of a small bioactive peptide of potential unse in Biotechnology
BERNINI A.;ROSSOLINI, GIAN MARIA;LOZZI, LUISA;NERI, PAOLO;NICCOLAI, NERI
1999-01-01
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. © 1999 Taylor & Francis Group, LLC.
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https://hdl.handle.net/11365/34351
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