All-D-cecropin B: synthesis, conformation, lipopolysaccharide binding, and antibacterial activity.
Cecropin B (LCB) is a natural peptide with antibacterial and antifungal properties. The enantiomer of LCB, containing all-D amino acids (DCB), was synthesized to examine its antibacterial and binding properties. The conformation of DCB was compared to its enantiomer by circular dichroism. Both the L- and D-peptides showed an identical induction of alpha-helical secondary structure. However, binding studies between Lipopolysaccharide (LPS) and DCB or LCB were studied with a dimethylmethylene blue spectrophotometric assay, showing the two enantiomeric peptides differed in their interaction with LPS. Antibacterial activity of DCB was determined against three Gram-negative bacteria, Pantoea agglomerans (ATCC 27996), Escherichia coli (ATCC 8739), and Pseudomonas aeruginosa (ATCC 17648), giving comparable results to LCB.
Bland
J M
JM
United States Department of Agriculture, Agricultural Research Service, Southern Regional Research Center, New Orleans, LA 70179, USA.
De Lucca
A J
AJ
Jacks
T J
TJ
Vigo
C B
CB
D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004926:Escherichia coli / Q000187:drug effects*; D006090:Gram-Negative Bacteria / Q000187:drug effects*; D066298:In Vitro Techniques; D019476:Insect Proteins / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D008070:Lipopolysaccharides / Q000378:metabolism* / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D010452:Peptide Biosynthesis; D011485:Protein Binding; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000187:drug effects*; D013237:Stereoisomerism
D019476:Insect Proteins; D008070:Lipopolysaccharides; C031162:cecropin B protein, Insecta