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.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Ragona L,Molinari H,Zetta L,Longhi R,Marchini D,Dallai R,Bernini LF,Lozzi L,Scarselli M,Niccolai Ndoi
10.1002/(SICI)1097-0282(199611)39:5%3C653::AID-BIPsubject
Has Abstractpub_date
1996-11-01 00:00:00pages
653-64issue
5eissn
0006-3525issn
1097-0282pii
10.1002/(SICI)1097-0282(199611)39:5<653::AID-BIP4>journal_volume
39pub_type
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