High resolution heteronuclear correlation NMR spectroscopy of an antimicrobial peptide in aligned lipid bilayers: peptide-water interactions at the water-bilayer interface.

ABSTRACT: High-resolution two-dimensional (2D) (1)H-(15)N heteronuclear correlation (HETCOR) spectroscopy has been used to characterize the structure and dynamics of (15)N-backbone labeled antimicrobial piscidin 1 (p1) oriented in "native-like" hydrated lipid bilayers. Piscidin belongs to a family of amphipatic cationic antimicrobial peptides, which are membrane-active and have broad spectrum antimicrobial activity on bacteria. When the (1)H chemical shifts are encoded by the (1)H-(15)N dipolar couplings, 2D dipolar-encoded HETCOR (i.e., de-HETCOR) solid-state NMR spectra yield high resolution (1)H and (15)N chemical shifts as well as (1)H-(15)N heteronuclear dipolar couplings. Several advantages of HETCOR and de-HETCOR techniques that emerge from our investigations could facilitate the atomic-level

SUBMITTER: Fu R 

PROVIDER: S-EPMC2752699 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature