title: The amphipathic alpha-helix concept. Application to the de novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin.
abstract: An original series of 12- to 22-residue-long peptides was developed, they are only constituted by apolar Leu and charged Lys residues periodically located in the sequence in order to general ideal highly amphipathic alpha-helices. By circular dichroism, the peptides are proven to be mainly alpha-helical in organic and aqueous solvents and in the presence of lipids. The peptides are highly hemolytic, their activity varies according to the peptide length. The 15-, 20-, and 22-residue-long-peptides have LD50 approximately 5 x 10(-8) M for 10(7) erythrocytes, i.e. they are 5-10 times more active than melittin, and are indeed several orders of magnitude more active than magainin or mastoparan.
authors.affiliation: Centre de Recherche Paul Pascal, CNRS, Pessac, France.
authors.forename: I
authors.initials: I
authors.lastname: Cornut
authors.forename: K
authors.initials: K
authors.lastname: Büttner
authors.forename: J L
authors.initials: JL
authors.lastname: Dasseux
authors.forename: J
authors.initials: J
authors.lastname: Dufourcq
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006460:Hemolysin Proteins / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D007930:Leucine / Q000737:chemistry; D008239:Lysine / Q000737:chemistry; D008555:Melitten / Q000737:chemistry / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
chemical_list: D006460:Hemolysin Proteins; D010455:Peptides; D008555:Melitten; D007930:Leucine; D008239:Lysine