Study of structure-activity relationship in Aurein 1.2 analogs.
Two new analogs of Aurein 1.2 antimicrobial peptide were synthesized and the antimicrobial activities were investigated. The results showed that the activity of G1R/F3W analog was higher than the native peptide and the F3W analog. Circular dichroism studies also showed that the secondary structure of the F3W was concentration-dependent, whereas, there was no such relationship seen in the case of G1R/F3W analog. It has been proposed that G1R/F3W activity was based on a single mechanism (snorkeling), while Aurein 1.2 and F3W utilized the snorkeling mechanism at low concentrations (0-0.01 mM) and the carpet mechanism at higher concentrations (0.01-0.1 mM). This study suggests that one pay attention to the concentration of biomolecules in peptide-based drug design.
Department of Biology, Payame Noor University, Arak 38195-466, Iran.
Safieh
S
Soufian
Leila
L
Hassani
D000890:Anti-Infective Agents / Q000737:chemistry / Q000378:metabolism; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism*; D002942:Circular Dichroism; D017433:Protein Structure, Secondary; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D013329:Structure-Activity Relationship; D013501:Surface-Active Agents / Q000737:chemistry
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D013501:Surface-Active Agents; C506635:aurein 1.2 peptide; D012967:Sodium Dodecyl Sulfate