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- W135702927 abstract "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 LD 50 ∼5 × 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." @default.
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- W135702927 date "1994-07-25" @default.
- W135702927 modified "2023-10-14" @default.
- W135702927 title "The amphipathic α‐helix concept" @default.
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- W135702927 doi "https://doi.org/10.1016/0014-5793(94)00621-0" @default.
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