Resumo

CARRENO, Luisa Fernanda  e  LOZANO, José Manuel. Structural exploration of antibacterial activity and hemolytic profiles of non-natural analogs of the antimicrobial peptide mastoparan MP-8. Rev. colomb. cienc. quim. farm. [online]. 2013, vol.42, n.1, pp.56-79. ISSN 0034-7418.

In this work the relevance of a systematic replacement of peptide-bonds on the Mastoparan MP-8 antimicrobial peptide to afford 27 new pseudopeptide analogues is reported. Results allowed to determine that pseudopeptides ψ-38617 (INLKALAALAK^d-[CH2NH]-RLL), ψ-38629(INLKA^d-[CH2NH]-LAALAKRLL) and ψ-38630 (INLK-[CH2NH]-ALAALAKRLL), showed an enhanced anti gam-negative bacterial properties, regarding the native Mastoparan MP-8 peptide, but maintaining a comparable activity against gram-positive bacteria. In addition, specific performed modifications on MP-8 sequence led three new molecules that completely abolished the hemolytic activity of the parent MP-8 peptide. All obtained molecules possess a high stability profile when tested against a severe proteolytic attack.

Palavras-chave : antimicrobial peptide; Mastoparan MP-8; hemolytic activity; stability.

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