Trichogin GA IV: an antibacterial and protease-resistant peptide.
The antibacterial and hemolytic activities of the amphiphilic helical, membrane-active, lipopeptaibol trichogin GA IV and its [Leu(11)-OMe] analogue were compared to those of the partially helical or non-helical 8-meric or 4-meric, C-terminal short sequences, respectively. The study on trichogin GA IV was extended to several methicillin-resistant Staphylococcus aureus strains. Using a large set of enzymes, we also evaluated the resistance to proteolysis of all of the four peptides.
De Zotti
Marta
M
Institute of Biomolecular Chemistry, Padova Unit, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy.
Biondi
Barbara
B
Formaggio
Fernando
F
Toniolo
Claudio
C
Stella
Lorenzo
L
Park
Yoonkyung
Y
Hahm
Kyung-Soo
KS
D023181:Antimicrobial Cationic Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects*; D002176:Candida albicans / Q000187:drug effects; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D006461:Hemolysis / Q000187:drug effects; D055666:Lipopeptides / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D008826:Microbial Sensitivity Tests; D010447:Peptide Hydrolases / Q000378:metabolism*
D023181:Antimicrobial Cationic Peptides; D055666:Lipopeptides; C116419:trichogin GA IV; D010447:Peptide Hydrolases