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This paper deals with the recent developments in the structure-function relationship of membrane-perturbing peptides and fusion peptides. Membrane-perturbing mechanism proposed for natural peptide magainin is first introduced followed by some properties including biological activity of designed membrane-perturbing peptides. Next, the interaction of peptides derived from natural fusion proteins and designed fusion peptides with lipids is described. These peptides have generally amphiphilic structure and their activities toward lipid and cell membranes highly depend on the hydrophobicity, hydrophobic moment and peptide sequence. In this connection, such amphiphilic peptides have been expected as new materials of gene carrier and endosome-disruptive compounds. Recent progress in peptide-mediated gene transfer technique and the advantage on usage of amphiphilic peptides as gene carrier are presented.