Previous investigations related to interactions with lipids have evidenced the importance of the conformational state of cell-penetrating peptides on the cellular internalization process [1-2].In order to understand the mechanism of the plasma membrane crossing,two peptides with similar sequences and but different structures were synthesized:The hydrophobic domain is a issued from fusion peptide GP41 of HIV1;some residues were substituted according to the AGADIR software in order to obtain the Palpha peptide which is predicted to adopt a helical conformation.
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