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Author(s): Vitor Teixeira
Maria J. Feio
Luis Rivas
Beatriz G. De la Torre
David Andreu
Ana Coutinho
Margarida Bastos
Title: Influence of Lysine Nε-Trimethylation and Lipid Composition on the Membrane Activity of the Cecropin A-Melittin Hybrid Peptide CA(1-7)M(2-9)
Issue Date: 2010
Abstract: Although many studies have pointed out the promising role of antimicrobial peptides (AMPs) as therapeuticalagents, their translation into clinical research is being slow due to the limitations intrinsic to their peptidenature. A number of structural modifications to overcome this problem have been proposed, leading to enhancedAMP biological lifetimes and therapeutic index. In this work, the interaction between liposomes of differentlipidic composition and a set of lysine Nε-trimethylated analogs of the cecropin A and melittin hybrid peptide,CA(1-7)M(2-9) [H-KWKLFKKIGAVLKVL-amide], was studied by differential scanning calorimetry (DSC)and fluorescence spectroscopy. The study was carried out using membrane models for mammalian erythrocytes(zwitterionic lipids) and for bacteria (mixture of zwitterionic and negatively charged lipids). The results showthat trimethylated peptides interact strongly with negatively charged (bacterial cell model) but not withzwitterionic (erythrocyte model) liposomes. These results are in agreement with the reduction of cytotoxicityand ensuing improvement in therapeutic index vs parental CA(1-7)M(2-9) found in a related study. Moreover,the modified peptides act differently depending on the model membrane used, providing further evidencethat the lipid membrane composition has important implications on AMP membrane activity.
Subject: Química aplicada, Química física, Engenharia química
Applied chemistry, Physical chemistry, Chemical engineering
Scientific areas: Ciências da engenharia e tecnologias::Engenharia química
Engineering and technology::Chemical engineering
Document Type: Artigo em Revista Científica Internacional
Rights: restrictedAccess
Appears in Collections:FCUP - Artigo em Revista Científica Internacional

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