CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity.

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

Biopolymers

journal_title

Biopolymers

authors

Ragona L,Molinari H,Zetta L,Longhi R,Marchini D,Dallai R,Bernini LF,Lozzi L,Scarselli M,Niccolai N

doi

10.1002/(SICI)1097-0282(199611)39:5%3C653::AID-BIP

subject

Has Abstract

pub_date

1996-11-01 00:00:00

pages

653-64

issue

5

eissn

0006-3525

issn

1097-0282

pii

10.1002/(SICI)1097-0282(199611)39:5<653::AID-BIP4>

journal_volume

39

pub_type

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