The amphipathic α‐helix concept

FEBS Letters

Büttner, Klaus¹  Dufourcq, Jean²  Cornut, Isabelle²  Dasseux, Jean-Louis¹ 

[1] Fournier Pharma GmbH, Justus von Liebig Strasse 16, 6603 Sulzbach, Germany;Centre de Recherche Paul Pascal, CNRS, Avenue Schweitzer, 33600 Pessac, France

关键词: Amphipathic helix;    Hemolysis;    Cytotoxic peptide;    LiKj;    peptide composed of i residues Leu and j residues Lys;    Dns;    dansyl;    Mel;    melittin;    Lyso-PC;    lysophosphatidylcholine;    DMPC;    dimyristoyl phosphatidylcholine;    SUV;    small unilamellar vesicles;    Hα;    α-helix;   

DOI  :  10.1016/0014-5793(94)00621-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An original serie 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 generate ideal highly amphipathic α-helices. By circular dichroism, the peptides are proven to be mainly α-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 ∼5 × 10⁻⁸ M for 10⁷ 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.

【 授权许可】

Unknown