Determining the Orientation and Localization of Membrane-Bound Peptides

Author(s): Walter Hohlweg , Simone Kosol , Klaus Zangger .

Journal Name: Current Protein & Peptide Science

Volume 13 , Issue 3 , 2012

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Abstract:

Many naturally occurring bioactive peptides bind to biological membranes. Studying and elucidating the mode of interaction is often an essential step to understand their molecular and biological functions. To obtain the complete orientation and immersion depth of such compounds in the membrane or a membrane-mimetic system, a number of methods are available, which are separated in this review into four main classes: solution NMR, solid-state NMR, EPR and other methods. Solution NMR methods include the Nuclear Overhauser Effect (NOE) between peptide and membrane signals, residual dipolar couplings and the use of paramagnetic probes, either within the membrane-mimetic or in the solvent. The vast array of solid state NMR methods to study membrane-bound peptide orientation and localization includes the anisotropic chemical shift, PISA wheels, dipolar waves, the GALA, MAOS and REDOR methods and again the use of paramagnetic additives on relaxation rates. Paramagnetic additives, with their effect on spectral linewidths, have also been used in EPR spectroscopy. Additionally, the orientation of a peptide within a membrane can be obtained by the anisotropic hyperfine tensor of a rigidly attached nitroxide label. Besides these magnetic resonance techniques a series of other methods to probe the orientation of peptides in membranes has been developed, consisting of fluorescence-, infrared- and oriented circular dichroism spectroscopy, colorimetry, interface-sensitive X-ray and neutron scattering and Quartz crystal microbalance.

Keywords: Antimicrobial peptides, immersion depth, membrane-bound peptides, NMR spectroscopy, orientation, paramagnetic relaxation enhancement, peptide hormones, toxins, membrane-bound peptides, NMR spectroscopy

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Article Details

VOLUME: 13
ISSUE: 3
Year: 2012
Page: [267 - 279]
Pages: 13
DOI: 10.2174/138920312800785049

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