Modification of the C terminus of cecropin is essential for broad-spectrum antimicrobial activity.
Antimicrob Agents Chemother
; 37(8): 1614-9, 1993 Aug.
Article
en En
| MEDLINE
| ID: mdl-8215272
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Péptidos Catiónicos Antimicrobianos
/
Hormonas de Insectos
/
Antibacterianos
Idioma:
En
Revista:
Antimicrob Agents Chemother
Año:
1993
Tipo del documento:
Article
Pais de publicación:
Estados Unidos