Microstructural characterization of lysophosphatidylcholine micellar aggregates: The structural basis for their use as biomembrane mimics

Vitiello, Giuseppe; Ciccarelli, Donato; Ortona, Ornella; D’Errico, Gerardino

doi:10.1016/j.jcis.2009.04.008

Cited by 19 publications

(18 citation statements)

References 38 publications

(54 reference statements)

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“…As of this writing, there are only a few lyso-PC aggregation numbers available from the literature. For C10 and C12 lyso-PCs, we determined aggregation numbers of 35/40 and 78/82 at a detergent concentration of 20 mM (Table 2), which are in good agreement with values determined by NMR spectroscopy (34 for C10 and 55 for C12 lyso-PC) (39).…”

Section: The Stability Of the Gpa Tm Domain Dimer Depends On The Lysosupporting

confidence: 81%

Detergent Properties Influence the Stability of the Glycophorin A Transmembrane Helix Dimer in Lysophosphatidylcholine Micelles

Stangl

Veerappan

Kroeger

et al. 2012

Biophysical Journal

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Detergents might affect membrane protein structures by promoting intramolecular interactions that are different from those found in native membrane bilayers, and fine-tuning detergent properties can be crucial for obtaining structural information of intact and functional transmembrane proteins. To systematically investigate the influence of the detergent concentration and acyl-chain length on the stability of a transmembrane protein structure, the stability of the human glycophorin A transmembrane helix dimer has been analyzed in lyso-phosphatidylcholine micelles of different acyl-chain length. While our results indicate that the transmembrane protein is destabilized in detergents with increasing chain-length, the diameter of the hydrophobic micelle core was found to be less crucial. Thus, hydrophobic mismatch appears to be less important in detergent micelles than in lipid bilayers and individual detergent molecules appear to be able to stretch within a micelle to match the hydrophobic thickness of the peptide. However, the stability of the GpA TM helix dimer linearly depends on the aggregation number of the lyso-PC detergents, indicating that not only is the chemistry of the detergent headgroup and acyl-chain region central for classifying a detergent as harsh or mild, but the detergent aggregation number might also be important.

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Section: The Stability Of the Gpa Tm Domain Dimer Depends On The Lysosupporting

confidence: 81%

Detergent Properties Influence the Stability of the Glycophorin A Transmembrane Helix Dimer in Lysophosphatidylcholine Micelles

Stangl

Veerappan

Kroeger

et al. 2012

Biophysical Journal

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“…Indeed, considering the data reported for DHPC (14 m M CMC and aggregation number N = 27), under our experimental conditions (500 µ M StI: 50 m M DHPC) we expect a fast exchange equilibrium between about 14 m M DHPC in the monomeric form, 22.5 m M DHPC in free micellar form, and 13.5 m M DHPC in micellar form complexed with StI (assuming a quantitative 1:1 complex formation). For the other lipid systems, the monomeric forms and free micelles are less likely to contribute to the measured diffusion coefficients, in view of the much smaller CMCs and the higher aggregation numbers reported in the literature (for 12C‐lysoPC the CMC is 1 m M and N = 55; for 16C‐lysoPC the CMC is 7 µ M ). The NMR spectra obtained in larger systems (12C‐lysoPC, 12C‐lysoPC/lysoSM, 16C‐lysoPC,) were useless (Supporting information Figs.…”

Section: Discussionmentioning

confidence: 99%

Solution NMR analysis of the interaction between the actinoporin Sticholysin I and DHPC micelles—Correlation with backbone dynamics

et al. 2013

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Sticholysin I (StI), an actinoporin expressed as a water-soluble protein by the sea anemone Stichodactyla helianthus, binds to natural and model membranes, forming oligomeric pores. It is proposed that the first event of a multistep pore formation mechanism consists of the monomeric protein attachment to the lipid bilayer. To date there is no high-resolution structure of the actinoporin pore or other membrane-bound form available. Here we evaluated StI:micelle complexes of variable lipid composition to look for a suitable model for NMR studies. Micelles of pure or mixed lysophospholipids and of dihexanoyl phosphatidylcholine (DHPC) were examined. The StI:DHPC micelle was found to be the best system, yielding a stable sample and good quality spectra. A comprehensive chemical shift perturbation analysis was performed to map the StI membrane recognition site in the presence of DHPC micelles. The region mapped (residues F(51), R(52), S(53) in loop 3; F(107), D(108), Y(109), W(111), Y(112), W(115) in loop 7; Q(129), Y(132), D(134), M(135), Y(136), Y(137), G(138) in helix-α2) is in agreement with previously reported data, but additional residues were found to interact, especially residues V(81), A(82), T(83), G(84) in loop 5, and A(85), A(87) in strand-β5. Backbone dynamics measurements of StI free in solution and bound to micelles highlighted the relevance of protein flexibility for membrane binding and suggested that a conformer selection process may take place during protein-membrane interaction. We conclude that the StI:DHPC micelles system is a suitable model for further characterization of an actinoporin membrane-bound form by solution NMR.

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“…LPC is a class of phospholipids characterized by a single acyl chain and thus exhibiting a surfactant-like behavior in solution (Figure 1). Indeed, while bi-tailed phospholipids such as POPC or DOPC, mainly form liposome in solution, LPC can form micelles (Vitiello et al, 2009). The dynamic nature of LPC micelles in solution makes the LPC molecules suitable candidates for NP coating (Luchini et al, 2016a).…”

Section: Strategies For Lipid Coating On Inorganic Nanoparticlesmentioning

confidence: 99%

Understanding the Nano-bio Interfaces: Lipid-Coatings for Inorganic Nanoparticles as Promising Strategy for Biomedical Applications

2019

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Inorganic nanoparticles (NPs) exhibit relevant physical properties for application in biomedicine and specifically for both the diagnosis and therapy (i.e. theranostic) of severe pathologies, such as cancer. The inorganic NP core is often not stable in aqueous suspension and can induce cytotoxic effects. For this reason, over the years, several coating strategies were suggested to improve the NP stability in aqueous solutions as well as the NP biocompatibility. Among the various components which can be used for NP coatings, lipids, and in particular phospholipids emerged as versatile molecular building blocks for the production of NP coatings suitable for biomedical application. The recent synthetic efforts in NP lipid coatings allows today to introduce on the NP surface a large variety of lipid molecules eventually in mixture with amphiphilic or hydrophobic drugs or active molecules for cell targeting. In this review, the most relevant examples of NP lipid-coatings are presented and grouped in two main categories: supported lipid bilayers (SLB) and hybrid lipid bilayers (HLB). The discussed scientific cases take into account the most commonly used inorganic NP for biomedical applications in cancer therapy and diagnosis.

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Microstructural characterization of lysophosphatidylcholine micellar aggregates: The structural basis for their use as biomembrane mimics

Cited by 19 publications

References 38 publications

Detergent Properties Influence the Stability of the Glycophorin A Transmembrane Helix Dimer in Lysophosphatidylcholine Micelles

Detergent Properties Influence the Stability of the Glycophorin A Transmembrane Helix Dimer in Lysophosphatidylcholine Micelles

Solution NMR analysis of the interaction between the actinoporin Sticholysin I and DHPC micelles—Correlation with backbone dynamics

Understanding the Nano-bio Interfaces: Lipid-Coatings for Inorganic Nanoparticles as Promising Strategy for Biomedical Applications

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