Antibiotic properties of novel synthetic temporin A analogs and a cecropin A-temporin A hybrid peptide.
Temporin A, 18 analogs, and a cecropin A-temporin A hybrid peptide were tested with antibiotic sensitive and resistant bacteria, fungi, human erythrocytes, and in clotting assays. Several peptides were active in these assays, and some analogs (D-TA, W1-TA, and Con-L4,G10) may be useful lead compounds for further antibiotics development. The activity of temporin A was found to be dependent upon several of its structural features, including amino acid composition and sequence, chirality, helicity, and positive charge.
Wade
David
D
Karolinska Institutet, Department of Microbiology, Pathology, and Immunology, Division of Clinical Virology, F-68, Huddinge University Hospital, S-14186 Huddinge, Sweden.
Flock
Jan-Ingmar
JI
Edlund
Charlotta
C
Löfving-Arvholm
Ingegerd
I
Sällberg
Matti
M
Bergman
Tomas
T
Silveira
Angela
A
Unson
Cecille
C
Rollins-Smith
Louise
L
Silberring
Jerzy
J
Richardson
Malcom
M
Kuusela
Pentti
P
Lankinen
Hilkka
H
D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000494:pharmacology*; D000935:Antifungal Agents / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000494:pharmacology*; D001681:Biological Assay; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D010455:Peptides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry / Q000494:pharmacology*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; D011506:Proteins; D011993:Recombinant Fusion Proteins; C104501:temporin; C031161:cecropin A