A new method for determining the local environment and orientation of individual side chains of membrane-binding peptides.
We studied here the binding of the mastoparan X peptide to a zwitterionic lipid bilayer (POPC) and demonstrated that nitrile-derivatized amino acids can be used to determine the hydration state (or change in hydration state) of specific sites of membrane-interactive peptides (upon binding). We have also shown that polarized ATR-FTIR measurements can further be used to uncover information regarding the spatial orientation of individual side chains as well as their conformational preference within the lipid bilayer.
Tucker
Matthew J
MJ
Department of Chemistry, University of Pennsylvania, Philadelphia, 19104 USA.
Getahun
Zelleka
Z
Nanda
Vikas
V
DeGrado
William F
WF
Gai
Feng
F
D000577:Amides / Q000737:chemistry; D002462:Cell Membrane / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013055:Spectrophotometry, Infrared
D000577:Amides; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010455:Peptides; D010743:Phospholipids