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  • Title: Liposomal cargo unloading induced by pH-sensitive peptides.
    Author: Lee HM, Chmielewski J.
    Journal: J Pept Res; 2005 Mar; 65(3):355-63. PubMed ID: 15787966.
    Abstract:
    Amphiphilic peptides designed to have a pH-dependent conformational change and membrane activity are described. At physiologic pH, the peptides would exist in a random coil conformation, but at endosomal pH values they would switch to amphiphilic alpha-helices, disrupt membranes, and release liposomal contents. A series of peptides have been investigated that contain a high percentage of Glu residues for the pH-induced conformational switch, and Leu residues for optimal lipid binding. Circular dichroism (CD) results in aqueous and liposomal environments were performed and demonstrate a pH-dependent shift to helicity upon acidification. Liposomal release data at neutral and acidic pH, also document the success of this design strategy.
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