Abstract
Anoplin, GLLKRIKTLL-NH2, isolated from the venom sac of solitary spider wasp, Anoplius samariensis, is the smallest linear α-helical antimicrobial peptide found naturally up to date. Previously Cabrera et al. (J. Pept. Sci. 2008) reported that deamidation dramatically decreased antimicrobial activity of the peptide and showed that amidated Anoplin forms pores in toroidal manner in anionic bilayer. In the present work, interactions of two forms of Anoplin (Anoplin-NH2 and Anoplin-COOH) with model cell membrane (zwitterionic DPPC, anionic DPPG or E. coli extract) were further investigated in order to gain a better understanding of the effect of amidations on the kinetics and thermodynamics of the peptide- membrane interactions. Langmuir Blodgett, Atomic Force Microscopy, UV resonance Raman spectroscopy and Calcein leakage assay were used. Results of the study indicate that amidated form of Anoplin has higher membrane binding activity.
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