All-D-cecropin B: Synthesis,conformation, lipopolysaccharide binding,and antibacterial activity |
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Authors: | Bland John M De Lucca Anthony J Jacks Tom J Vigo Craig B |
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Institution: | (1) United States Department of Agriculture, Agricultural Research Service, Southern Regional Research Center, P.O. Box 19687, New Orleans, LA 70179, USA |
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Abstract: | 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 -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. |
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Keywords: | all-D-cecropin solid phase peptide synthesis circular dichroism conformation lipopolysaccharide binding antibacterial activity |
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