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|Title:||CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity||Authors:||Ragona, L
BERNINI L., F
|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.
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