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. 1993 Aug;37(8):1614–1619. doi: 10.1128/aac.37.8.1614

Modification of the C terminus of cecropin is essential for broad-spectrum antimicrobial activity.

J E Callaway 1, J Lai 1, B Haselbeck 1, M Baltaian 1, S P Bonnesen 1, J Weickmann 1, G Wilcox 1, S P Lei 1
PMCID: PMC188029  PMID: 8215272

Abstract

Cecropin A is a naturally occurring peptide with bactericidal activity against gram-negative and gram-positive bacteria. Production of large quantities of bactericidal peptides that are similar in structure and activity to cecropin A has been achieved by combining recombinant DNA techniques and techniques and chemical modification. Expression of the bactericidal peptide in Escherichia coli was accomplished through the formation of a fusion protein. The 5' end of the L-ribulokinase gene was fused to a single copy of a synthetic gene encoding cecropin A. A methionine codon was engineered between the two genes, and a methionylglycine extension was introduced at the C terminus of cecropin A. Cyanogen bromide treatment of the fusion protein yielded cecropin A with a C-terminal homoserine. The recombinant cecropin A with a homoserine at the C terminus did not kill most gram-positive bacteria tested. However, recombinant cecropin A with a chemically modified C terminus has antimicrobial activity similar to that of cecropin produced by cecropia pupae.

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Selected References

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