Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4162
Title: CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity
Authors: Ragona, L
Molinari, H
Zetta, L
Longhi, R
Marchini, Daniela
Dallai, R
BERNINI L., F
Lozzi, Luisa
Scarselli, M
Niccolai, Neri 
Keywords: INSECT IMMUNITY, REPRODUCTIVE ACCESSORY-GLANDS, NUCLEAR MAGNETIC-RESONANCE, RESTRAINED MOLECULAR-DYNAMICS, MEDFLY CERATITIS-CAPITATA, PHOSPHOLIPID-MEMBRANES, SOLUTION CONFORMATION, PROTEIN-STRUCTURE, FROG-SKIN, HELIX
Issue Date: 1996
Project: None 
Journal: BIOPOLYMERS
Abstract: 
Antibacterial properties of the secretion from the female reproductive accessory glands of medfly Ceratitis capitata are mostly ascribed to the presence of two peptides, ceratotoxin A and B, which exhibit a strong activity against gram-positive and gram-negative bacterial strains, and show sequence and function homology with cecropins, melittin, and magainins. CD experiments performed in different solvents indicate the presence of a significant content of helical structures in organic solvent. Two-dimensional nmr results for ceratotoxin A in methanol show a helical behavior for the 8-25 region of the peptide. A Ramachandran classification of each residue for the structures obtained from distance geometry calculations lead to the definition of four structural families in which the central segment 10-19 is always helical and differences refer to residues 8-9 and 19-23. A sequence analysis of the two ceratotoxins and a systematic search on the protein data bank revealed the occurrence of a KX-hydrophobic-hydrophobic-P motif that seems to be important for helix stabilization.
Description: 
37587
URI: http://hdl.handle.net/20.500.12779/4162
ISSN: 0006-3525
DOI: 10.1002/(SICI)1097-0282(199611)39:5<653
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