<sup>31</sup>P-NMR Methods for Investigating Phospholipid-Based Molecular Structure and Dynamics

Dufourc, Érick J.; Maillet, Jean-Christophe; Pott, Tanja; Léonard, A.

doi:10.1080/10426509308045634

Cited by 3 publications

(6 citation statements)

References 5 publications

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“…To model the overproduction of Bcl-2 found in cancer processes, we studied the impact of elevated concentrations of its regulative BH4 segment on these mitochondrial membranes from the peptide and lipid perspective. Combined solid state 2 H-NMR and differential scanning calorimetry revealed the coexistence of small sized fluid and rigid membrane domains over a large temperature range, which is confirmed by 31 P-NMR at 30°C. The latter are stabilized, in a cholesterol-like manner, by the presence of a BH4 peptide.…”

mentioning

confidence: 71%

“…In Fig. 5A, the 31 P static spectrum of MLV vesicles composed of DMPC ⁄ DMPG at a 2 : 1 molar ratio exhibits a typical pattern of lipid bilayers in a liquid crystalline phase at 30°C. It is dominated by the chemical shift anisotropy (CSA) of the phosphate groups from both PC and phosphoglycerol (PG), partially averaged by fast axial rotation [33,45].…”

Section: N-nmrmentioning

confidence: 99%

“…The number of scans collected for static 14 N-NMR did not exceed 250 000. 31 P MAS NMR experiments were acquired under proton decoupling (40 kHz) using a single p ⁄ 2-pulse with a duration of 6.5 ls. A Hahn echo sequence was applied for 31 P static measurements with an interpulse delay of 50 ls.…”

Section: Dscmentioning

confidence: 99%

“…31 P MAS NMR experiments were acquired under proton decoupling (40 kHz) using a single p ⁄ 2-pulse with a duration of 6.5 ls. A Hahn echo sequence was applied for 31 P static measurements with an interpulse delay of 50 ls. All 31 P spectra were referenced externally to )0.9 p.p.m., using DMPC vesicles at 308°K.…”

Section: Dscmentioning

confidence: 99%

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Restriction of lipid motion in membranes triggered by β‐sheet aggregation of the anti‐apoptotic BH4 domain

et al. 2008

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The regulative BH4 domain of human Bcl‐2 protein exerts its anti‐apoptic activity via the mitochondrion. In the present study, we investigated the molecular interactions of this domain with negatively charged liposomes mimicking the outer mitochondrial membrane. To model the overproduction of Bcl‐2 found in cancer processes, we studied the impact of elevated concentrations of its regulative BH4 segment on these mitochondrial membranes from the peptide and lipid perspective. Combined solid state 2H‐NMR and differential scanning calorimetry revealed the coexistence of small sized fluid and rigid membrane domains over a large temperature range, which is confirmed by 31P‐NMR at 30 °C. The latter are stabilized, in a cholesterol‐like manner, by the presence of a BH4 peptide. In the same time scale, the reduction of the headgroup order is seen in the static 14N and 31P‐NMR spectra when BH4 inserts into the bilayers. Indeed, attenuated total reflection spectroscopy indicated a dominant aggregated β‐sheet secondary structure of BH4 with a 42° tilt relative to the membrane surface. These results are discussed in terms of membrane stabilization versus apoptotic mechanisms at the outer mitochondrial membrane location.

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mentioning

confidence: 71%

Section: N-nmrmentioning

confidence: 99%

Section: Dscmentioning

confidence: 99%

Section: Dscmentioning

confidence: 99%

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Restriction of lipid motion in membranes triggered by β‐sheet aggregation of the anti‐apoptotic BH4 domain

et al. 2008

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“…This is more likely due to the different shape encountered in MLVs compared to isolated mitochondria. Despite the membrane still displaying a bilayer organization, the phospholipids experience different curvature constraints, which can modulate their headgroup orientation (22,23). Static 31 P NMR does not allow observation of individual phospholipid components in the mitochondrial membrane, due to the spectral overlapping of powder patterns originating from each lipid.…”

Section: P Nmr Spectroscopy: Integrity Of Isolated Mitochondria and Tmentioning

confidence: 99%

Magic‐angle phosphorus NMR of functional mitochondria:in situmonitoring of lipid response under apoptotic‐like stress

et al. 2009

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Using a noninvasive, solid-state magic-angle spinning nuclear magnetic resonance (MAS NMR) approach, we track ex vivo the behavior of individual membrane components in isolated, active mitochondria (model system: potato tubers) during physiological processes. The individual phosphatidylcholine (PC), phosphatidylethanolamine (PE), and cardiolipin (CL) membrane constituents were identified as distinct lines by applying MAS (31)P NMR on extracted lipid membranes. However, the CL NMR signal appeared to be very broad in functional mitochondria, indicating a tight complex formation with membrane protein. Calcium stress induced severe membrane degradation without recovery of a single CL NMR resonance. This suggests that calcium overload destroys the outer mitochondrial membrane and does not modify strongly the CL protein complexes in the inner membrane; a conclusion confirmed by respiratory controls. Conversely, mitochondrial membrane disruption on time degradation or mechanical stress generates clearly visible identical CL NMR signals, similar to those observed in rehydrated lipid extracts. Similarly, noninvasive based NMR tracking of lipids in response to diverse physiological stimuli can easily be used for other organelles and whole living cells.

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NMR methods for studying membrane‐active antimicrobial peptides

Strandberg

Ulrich

2004

Concepts Magnetic Resonance

142

117

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NMR is a versatile tool for studying interactions between antimicrobial peptides and lipid membranes. Different approaches using both liquid state and solid state NMR are outlined here, with an emphasis on solid state NMR methods, to study the structures of antimicrobial peptides in lipid bilayers as well as the effect of these peptides on model membranes. Different NMR techniques for observing both peptides and lipids are explained, including

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³¹P-NMR Methods for Investigating Phospholipid-Based Molecular Structure and Dynamics

Cited by 3 publications

References 5 publications

Restriction of lipid motion in membranes triggered by β‐sheet aggregation of the anti‐apoptotic BH4 domain

Restriction of lipid motion in membranes triggered by β‐sheet aggregation of the anti‐apoptotic BH4 domain

Magic‐angle phosphorus NMR of functional mitochondria:in situmonitoring of lipid response under apoptotic‐like stress

NMR methods for studying membrane‐active antimicrobial peptides

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31P-NMR Methods for Investigating Phospholipid-Based Molecular Structure and Dynamics

Cited by 3 publications

References 5 publications

Restriction of lipid motion in membranes triggered by β‐sheet aggregation of the anti‐apoptotic BH4 domain

Restriction of lipid motion in membranes triggered by β‐sheet aggregation of the anti‐apoptotic BH4 domain

Magic‐angle phosphorus NMR of functional mitochondria:in situmonitoring of lipid response under apoptotic‐like stress

NMR methods for studying membrane‐active antimicrobial peptides

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Product

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³¹P-NMR Methods for Investigating Phospholipid-Based Molecular Structure and Dynamics