A modification of the N-terminal amino acid in the eremomycin aglycone.
An Edman degradation of the antibiotic eremomycin aglycone produced the corresponding hexapeptide, which was aminoacylated with D-lysine, D-histidine or D-tryptophan derivatives to give new heptapeptide analogs of the eremomycin aglycone. The aminoacylation of the eremomycin aglycone produced an octapeptide analog. The substitution of D-lysine for the N-terminal N-methyl-D-leucine does not seriously affect the in vitro antibacterial properties of the eremomycin aglycone whereas the heptapeptides with the N-terminal D-tryptophan or D-histidine moieties and the octapeptide with the N-terminal D-lysine are practically devoid of the antibacterial properties.
Miroshnikova
O V
OV
Institute of New Antibiotics, Russian Academy of Medical Sciences, Moscow, Russia.
Berdnikova
T F
TF
Olsufyeva
E N
EN
Pavlov
A Y
AY
Reznikova
M I
MI
Preobrazhenskaya
M N
MN
Ciabatti
R
R
Malabarba
A
A
Colombo
L
L
D000900:Anti-Bacterial Agents / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D006020:Glycopeptides; D008826:Microbial Sensitivity Tests; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D006020:Glycopeptides; D010455:Peptides; C053759:eremomycin; C057759:eremomycin aglycone