Recent discoveries have established that cationic peptides have the capacity to penetrate living cells and can serve as co-transporters of bioactive molecules via internalization processes. Such peptides are referred to as Cell Penetrating Peptides (CPP). We have observed the interaction of the CPP (RRWWRRWRR-NH2), a cationic peptide modified and equipped with one ferrocene, serving as redox probe, and biotin (sulfone), with Large Unilamellar Vesicles (LUVs) of different composition. Such observations can provide insight into the internalization processes. This study aimed at 1) developing detection systems of peptides present in complex environments; 2) measuring the amount of cationic peptides that cross the lipid bilayers, and 3) studying the influence of lipid composition and structure of the peptides on internalization. The results obtained on the interaction of (RW)9 with vesicles will help in the understanding of the function and internalization processes of the CPP (RW)9 yielding applications to intracellular pharmacology.

Electrochemical studies of cell penetrating peptide interactions with lipid membranes

243rd National Meeting (2012)

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