31P NMR Studies of Phospholipids

Филиппов, А. В.; Khakimov, A. M.; Munavirov, Bulat

doi:10.1016/bs.arnmr.2014.12.001

Cited by 16 publications

(19 citation statements)

References 122 publications

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“…This peak broadening arises from both heterogeneity in the local environment and also decreases in spin coherence times due to strong dipolar interactions between motion-restricted, closely packed lipids in the vesicle walls. 41,42 The SUVs that were exposed to amino-functionalized DNPs (Figure 3b−f) show further line broadening (from 5.0 ppm to 8.7 ± 1.9 ppm FWHM) and a small shoulder at −9 ppm. Previous studies have shown that line broadening occurs and is sensitive to mobility 39,43,44 or symmetry 40 changes of the lipids from SUV complexes.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Influence of Surface Ligand Molecular Structure on Phospholipid Membrane Disruption by Cationic Nanoparticles

et al. 2021

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Cationic nanoparticles are known to interact with biological membranes and often cause serious membrane damage. Therefore, it is important to understand the molecular mechanism for such interactions and the factors that impact the degree of membrane damage. Previously, we have demonstrated that spatial distribution of molecular charge at cationic nanoparticle surfaces plays an important role in determining the cellular uptake and membrane damage of these nanoparticles. In this work, using diamond nanoparticles (DNPs) functionalized with five different amine-based surface ligands and small phospholipid unilamellar vesicles (SUVs), we further investigate how chemical features and conformational flexibility of surface ligands impact nanoparticle/membrane interactions. 31P-NMR T 2 relaxation measurements quantify the mobility changes in lipid dynamics upon exposing the SUVs to functional DNPs, and coarse-grained molecular dynamics simulations further elucidate molecular details for the different modes of DNP–SUV interactions depending on the surface ligands. Collectively, our results show that the length of the hydrophobic segment and conformational flexibility of surface ligands are two key factors that dictate the degree of membrane damage by the DNP, while the amount of surface charge alone is not predictive of the strength of interaction.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Influence of Surface Ligand Molecular Structure on Phospholipid Membrane Disruption by Cationic Nanoparticles

et al. 2021

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“…Static wide-line and magic-angle spinning 31 P, 2 H, and 1 H NMR have been extensively used to study phospholipid bilayer organization and dynamics. 61,62 More specifically, 31 P NMR reports on the local environment and mobility of phospholipid head groups, whereas 1 H NMR reports on the mobility of both head groups and lipid chains. Here, we probed liposomal membrane dynamics by static 31 P and 1 H NMR.…”

Section: Characterization Of Liposome Preparations By Cryo-tem and Dlsmentioning

confidence: 99%

Nuclear Magnetic Resonance Spectroscopy: A Multifaceted Toolbox to Probe Structure, Dynamics, Interactions, and Real-Time In Situ Release Kinetics in Peptide-Liposome Formulations

et al. 2021

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Liposomal formulations represent attractive biocompatible and tunable drug delivery systems for peptide drugs. Among the tools to analyze their physicochemical properties, nuclear magnetic resonance (NMR) spectroscopy, despite being an obligatory technique to characterize molecular structure and dynamics in chemistry as well as in structural biology, yet appears to be rather sparsely used to study drug-liposome formulations. In this work, we exploited several facets of liquid-state NMR spectroscopy to characterize liposomal delivery systems for the apelin-derived K14P peptide and K14P modified by Nα-fatty acylation. Various liposome compositions and preparation modes were analyzed. Using NMR, in combination with cryo-electron microscopy and dynamic light scattering, we determined structural, dynamic, and self-association properties of these peptides in solution and probed their interactions with liposomes. Using 31P and 1H NMR, we characterized membrane fluidity and thermotropic phase transitions in empty and loaded liposomes. Based on diffusion and 1H NMR experiments, we localized and quantified peptides with respect to the interior/exterior of liposomes and changes over time and upon thermal treatments. Finally, we assessed the release kinetics of several solutes and compared various formulations. Taken together, this work shows that NMR has the potential to assist the design of peptide/liposome systems and more generally drug delivery systems.

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“…Relaxation measurements, such as T 1 and T 2 , report on motions of molecules on different timescales. For 31 P relaxation times, changes in T 1 report primarily on the dynamics of individual lipids while changes in T 2 reflect the collective motions of the bilayer [38]. 13 C and 15 N labelled Aβ peptides exhibit beta-sheet fibril [39] or disordered aggregate structure in model membrane environment, respectively.…”

Section: Solid-state Nmrmentioning

confidence: 99%

Section: Solid-state Nmrmentioning

confidence: 99%

Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides

Rajput

Sani

Keizer

et al. 2021

Biochemical Society Transactions

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Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of Aβ peptide aggregates. The amyloid plaques and soluble oligomeric species of Aβ are believed to be the major cause of synaptic dysfunction in AD brain and their cytotoxic mechanisms have been proposed to involve interactions with cell membranes. In this review, we discuss our solid-state nuclear magnetic resonance (ssNMR) studies of Aβ interactions with model membranes.

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31P NMR Studies of Phospholipids

Cited by 16 publications

References 122 publications

Influence of Surface Ligand Molecular Structure on Phospholipid Membrane Disruption by Cationic Nanoparticles

Influence of Surface Ligand Molecular Structure on Phospholipid Membrane Disruption by Cationic Nanoparticles

Nuclear Magnetic Resonance Spectroscopy: A Multifaceted Toolbox to Probe Structure, Dynamics, Interactions, and Real-Time In Situ Release Kinetics in Peptide-Liposome Formulations

Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides

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