Functional domain and poly-L-proline II conformation for candidacidal activity of bactenecin 5.
The functional domain for candidacidal activity of bactenecin 5 has been determined by synthesizing bactenecin 5 and its fragments [1-22 (BN22), 7-22 (BN16) and 20-43 (BC24)]. The N-terminal sequence BN16 retained the candidacidal potency of the parent molecule and this region appears to be the candidacidal domain. The circular dichroism spectra of these peptides indicate the presence of largely poly-L-proline II conformations in aqueous solutions and in lipid vesicles. The coupling constant (JNH-C alpha H) values, and a set of medium- and short-range nuclear Overhauser effects observed for the N-terminal peptide (BN16) in the two-dimensional nuclear magnetic resonance suggest that poly-L-proline II helix could be the biologically active conformation.
Raj
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PA
Department of Oral Biology, State University of New York at Buffalo 14214, USA.
Edgerton
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D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000737:chemistry* / Q000494:pharmacology; D002176:Candida albicans / Q000187:drug effects*; D002942:Circular Dichroism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000494:pharmacology; D011487:Protein Conformation
D000935:Antifungal Agents; D010455:Peptides; D010456:Peptides, Cyclic; C056454:bactenecin; C011083:polyproline