title: On the structural stability of a small bioactive peptide of potential use in biotechnology.
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.
authors.affiliation: Dipartimento di Biologia Molecolare, Università di Siena, Italy.
authors.forename: D
authors.initials: D
authors.lastname: Di Maro
authors.forename: M
authors.initials: M
authors.lastname: Scarselli
authors.forename: A
authors.initials: A
authors.lastname: Bernini
authors.forename: S
authors.initials: S
authors.lastname: Cresti
authors.forename: G M
authors.initials: GM
authors.lastname: Rossolini
authors.forename: L
authors.initials: L
authors.lastname: Lozzi
authors.forename: P
authors.initials: P
authors.lastname: Neri
authors.forename: N
authors.initials: N
authors.lastname: Niccolai
mesh_terms: D001709:Biotechnology / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides