On the structural stability of a small bioactive peptide of potential use in biotechnology

Daniela Di Maro, Maria Scarselli, Andrea Bernini, Stefania Cresti, Gian Maria Rossolini, Luisa Lozzi, Paolo Neri, Neri Niccolai

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)1053-1059
Number of pages7
JournalJournal of Biomolecular Structure and Dynamics
Volume16
Issue number5
Publication statusPublished - 1999

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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  • 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.