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