Molecular and Cellular Biochemistry

, Volume 218, Issue 1, pp 105–111

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

  • John M. Bland
  • Anthony J. De Lucca
  • Tom J. Jacks
  • Craig B. Vigo
Article

DOI: 10.1023/A:1007293816634

Cite this article as:
Bland, J.M., De Lucca, A.J., Jacks, T.J. et al. Mol Cell Biochem (2001) 218: 105. doi:10.1023/A:1007293816634

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 α-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.

all-D-cecropinsolid phase peptide synthesiscircular dichroism conformationlipopolysaccharide bindingantibacterial activity

Copyright information

© Kluwer Academic Publishers 2001

Authors and Affiliations

  • John M. Bland
    • 1
  • Anthony J. De Lucca
    • 1
  • Tom J. Jacks
    • 1
  • Craig B. Vigo
    • 1
  1. 1.United States Department of Agriculture, Agricultural Research ServiceSouthern Regional Research CenterNew OrleansUSA