Anti-plasmodial action of de novo-designed, cationic, lysine-branched, amphipathic, helical peptides.

ABSTRACT:

Background

A lack of vaccine and rampant drug resistance demands new anti-malarials.

Methods

In vitro blood stage anti-plasmodial properties of several de novo-designed, chemically synthesized, cationic, amphipathic, helical, antibiotic peptides were examined against Plasmodium falciparum using SYBR Green assay. Mechanistic details of anti-plasmodial action were examined by optical/fluorescence microscopy and FACS analysis.

Results

Unlike the monomeric decapeptides {(Ac-GXRKXHKXWA-NH2) (X = F,ΔF) (Fm, ΔFm IC50 >100 μM)}, the lysine-branched,dimeric versions showed far greater potency {IC50 (μM) Fd 1.5 , ΔFd 1.39}. The more helical and proteolytically stable ΔFd was studied for mechanistic details. ΔFq, a K-K2 dendrimer of ΔFm and (ΔFm)2 a linear dimer of ΔFm showed IC

SUBMITTER: Kaushik NK 

PROVIDER: S-EPMC3502156 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature