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- W2037858741 abstract "Interactions between a short synthetic antimicrobial peptide pEM-2 composed of 13 amino acid residues (KKWRWWLKALAKK) derived from C-terminus of myotoxin II of Bothrops asper and model membrane were investigated by Langmuir Blodgett (LB) and Atomic Force Microscopy (AFM). Peptide- induced surface area increase at constant pressure was studied for monolayers of zwitterionic DPPC, anionic DPPG phospholipids and E-coli extract. Increase in the transition state pressure for DPPG monolayer with increasing pEM-2 concentration and the corresponding AFM images show miscibility between the peptide and anionic lipid. It was found that incorporation of the peptide into DPPG monolayers is 2-3- orders of magnitude faster than into DPPC. The results indicate that electrostatic interactions play a significant role in the pEM-2-membrane interactions." @default.
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- W2037858741 date "2009-02-01" @default.
- W2037858741 modified "2023-09-28" @default.
- W2037858741 title "Molecular Mechanism of pEM-2 Activity" @default.
- W2037858741 doi "https://doi.org/10.1016/j.bpj.2008.12.704" @default.
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