Antimicrobial  peptides and peripheral membrane proteins are agents that shape and  mold their heterogeneous, interfacial environments through site-specific  noncovalent interactions with both aqueous and non-aqueous phases. The  variable water exposure of particular sites in these species can be  shown by several kinds of reporter groups, with none quite as small and  non-perturbative as vibrational probes located on selected side chains.  The CN stretching vibration of the artificial amino acid cyanylated  cysteine can report variable exposure to solution and membrane phases,  including the local hydration distribution of the labeled side chain.  This reporting ability will be used to detail the pore formation  mechanism of the antimicrobial peptide CM15 in bacterial membranes, and  also to document the flexible membrane-bound structures of  alpha-synuclein in contact with lipids of varying rigidity and  curvature.

Cyanylated cysteine as interfacial reporter in lipid-molding proteins

243rd National Meeting (2012)

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