Application of One-Dimensional Dipolar Shift Solid-State NMR Spectroscopy To Study the Backbone Conformation of Membrane-Associated Peptides in Phospholipid Bilayers

Lee, D. K.; Santos, Jose S.; Ramamoorthy, Ayyalusamy

doi:10.1021/jp9914929

Cited by 43 publications

(35 citation statements)

References 60 publications

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“…A 1-D dipolar-shift powder pattern, shown in Figure 3D, was used to determine the orientation of the chemical shielding tensor relative to the 15 N-labeled residues in magainin and pardaxin (42,43,50). The line shape depends strongly on the strength of the dipolar coupling and the angle so these parameters are determined precisely with this method, but R cannot be determined as precisely because the line shape varies only slightly with R for small values of , as is the case here (42,43). These parameters, determined from the solid powder spectra, were used to interpret the spectra of LL-37-L in oriented lipid bilayers.…”

Section: Resultsmentioning

confidence: 99%

Mechanism of Lipid Bilayer Disruption by the Human Antimicrobial Peptide, LL-37

2003

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LL-37 is an amphipathic, R-helical, antimicrobial peptide. 15 N chemical shift and 15 N dipolarshift spectroscopy of site-specifically labeled LL-37 in oriented lipid bilayers indicate that the amphipathic helix is oriented parallel to the surface of the bilayer. This surface orientation is maintained in both anionic and zwitterionic bilayers and at different temperatures and peptide concentrations, ruling out a barrelstave mechanism for bilayer disruption by LL-37. In contrast, electrostatic factors, the type of lipid, and the presence of cholesterol do affect the extent to which LL-37 perturbs the lipids in the bilayer as observed with 31 P NMR. The 31 P spectra also show that micelles or other small, rapidly tumbling membrane fragments are not formed in the presence of LL-37, excluding a detergent-like mechanism. LL-37 does increase the lamellar to inverted hexagonal phase transition temperature of both PE model lipid systems and Escherichia coli lipids, demonstrating that it induces positive curvature strain in these environments. These results support a toroidal pore mechanism of lipid bilayer disruption by LL-37.

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Section: Resultsmentioning

confidence: 99%

Mechanism of Lipid Bilayer Disruption by the Human Antimicrobial Peptide, LL-37

2003

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“…A variable temperature solid-state 15 N NMR study on lipid vesicles containing magainin 2 revealed its backbone dynamics [352]. The backbone dynamics of a channel-forming second-transmembrane segment of GABA receptor in lipid bilayers has been determined using PISEMA experiments [353].…”

Section: Insights Into Biological Problemsmentioning

confidence: 99%

Chemical shift tensor – The heart of NMR: Insights into biological aspects of proteins

Saitô¹,

Ando

Ramamoorthy

2010

Progress in Nuclear Magnetic Resonance Spectroscopy

182

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“…For example, it is difficult to establish an experimental condition that efficiently transfers magnetization from protons to carbons (or other low sensitive nuclei) at all sites of a molecule, and also for all molecules, in a bicelle sample. A short contact time crosspolarization (CP) [10] sequence is more efficient for rigid parts of a molecule than for mobile regions, as heteronuclear dipolar couplings in the latter case are averaged by the motion [11,12]. On the other hand, a long contact time or the NOE (nuclear Overhauser effect)-type magnetization transfer may be better for mobile sites of a molecule [13].…”

Section: Introductionmentioning

confidence: 99%

Sensitivity and resolution enhancement in solid-state NMR spectroscopy of bicelles

Dvinskikh

Yamamoto

Dürr

et al. 2007

Journal of Magnetic Resonance

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Magnetically aligned bicelles are becoming attractive model membranes to investigate the structure, dynamics, geometry, and interaction of membrane-associated peptides and proteins using solution- and solid-state NMR experiments. Recent studies have shown that bicelles are more suitable than mechanically aligned bilayers for multidimensional solid-state NMR experiments. In this work, we describe experimental aspects of the natural abundance (13)C and (14)N NMR spectroscopy of DMPC/DHPC bicelles. In particular, approaches to enhance the sensitivity and resolution and to quantify radio-frequency heating effects are presented. Sensitivity of (13)C detection using single pulse excitation, conventional cross-polarization (CP), ramp-CP, and NOE techniques are compared. Our results suggest that the proton decoupling efficiency of the FLOPSY pulse sequence is better than that of continuous wave decoupling, TPPM, SPINAL, and WALTZ sequences. A simple method of monitoring the water proton chemical shift is demonstrated for the measurement of sample temperature and calibration of the radio-frequency-induced heating in the sample. The possibility of using (14)N experiments on bicelles is also discussed.

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Application of One-Dimensional Dipolar Shift Solid-State NMR Spectroscopy To Study the Backbone Conformation of Membrane-Associated Peptides in Phospholipid Bilayers

Cited by 43 publications

References 60 publications

Mechanism of Lipid Bilayer Disruption by the Human Antimicrobial Peptide, LL-37

Mechanism of Lipid Bilayer Disruption by the Human Antimicrobial Peptide, LL-37

Chemical shift tensor – The heart of NMR: Insights into biological aspects of proteins

Sensitivity and resolution enhancement in solid-state NMR spectroscopy of bicelles

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