Abstract
The peptide cateslytin (RSMRLSFRARGYGFR) produced by enzymatic degradation of stress proteins is remarkably active against a large number of microorganisms including Plasmodium Falciparum responsible for Malaria. Its mode of action on membranes mimicking the external negatively charged membrane of these microorganisms has been studied by circular dichroism, infra-red (attenuated total reflection), high-resolution magic angle sample spinning and wide line solid state NMR, patch clamp and molecular dynamics. The peptide, which is unstructured in solution, adopts an aggregated beta sheet structure upon interacting with negatively charged membranes. Rigid membrane domains are formed upon interaction and separate from more fluid zwitterionic membrane zones. No macroscopic membrane lysis is observed, suggesting that crossing through membranes occurs at phase boundary defects. Patch clamp and all atom molecular dynamics of these zones indicate that disordered pores of ca. 10 Angstrom are formed by a mechanism that is analogous to molecular electroporation (Jean-Francois et al., Biochemistry & Biophysical J., 2008).View Large Image | View Hi-Res Image | Download PowerPoint Slide
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