Cardiolipin is one of the main components of the mitochondrial membrane while cholesterol is one of the principal components of lipid rafts in cell and model membranes. This project investigates the interaction of the cell penetrating peptide (CPP) Pep-1 with cardiolipin with and without cholesterol using infrared (IR), thermogravimetric analysis (TGA), and differential scanning calorimetry (DSC). Infrared data indicate that Pep-1 adopts a major helix conformation in the absence of cardiolipin. In the presence of cardiolipin, the content of the helix structure decreases with the peptide/cardiolipin molar ratio, but it remains helical. Upon cholesterol addition, Pep-1 adopts a major sheet conformation.TGA data indicate that cholesterol destabilizes the peptide/cardiolipin complex at any cholesterol concentration. TGA data also reveal that the two lipid systems form a non-ideal system, and the lipid acyl chain is affected by the presence of Pep-1. DSC reveals that Pep-1 induces anionic lipid clustering. The results obtained here provide a better understanding of the lipid-peptide interactions and can be used to assess the entry mechanism of Pep-1 in the bacteria

The effect of cholesterol on the interaction between Pep-1 and cardiolipin

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