PMID: 11330824May 2, 2001Paper

All-D-cecropin B: synthesis, conformation, lipopolysaccharide binding, and antibacterial activity

Molecular and Cellular Biochemistry
J M BlandC B Vigo

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 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.

Citations

Nov 7, 2001·Journal of Peptide Science : an Official Publication of the European Peptide Society·P StaubitzR W Jack
Jan 27, 2011·Chemical Biology & Drug Design·Troels GodballeHåvard Jenssen
Jun 16, 2012·The Journal of Biological Chemistry·Yang BaiKonstantin Pervushin
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