On the Structure, Dynamics and Possible Functional Roles of Inverted Micelles in Biological Membranes

Montal, Mauricio

doi:10.1007/978-1-4757-6424-6_21

Cited by 10 publications

(10 citation statements)

References 38 publications

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“…These versatile systems are employed in a broad range of technological applications. They can, for example, serve as vehicles for drug delivery, be used as chemical nanoreactors, and be applied to the controlled synthesis of materials and nanoparticles. , In addition, RMs are paradigm systems to investigate the effects of nanoscale confinement, for example, on the structural and dynamical properties of water , and on the protein folding and unfolding equilibrium. − They have been studied with a broad range of techniques, including nuclear magnetic resonance (NMR), − small-angle X-ray scattering (SAXS), small angle neutron scattering (SANS), , ultrafast infrared spectroscopy, − and numerical simulations. − This has, for example, led to a detailed characterization of the progressive slowdown of water dynamics with decreasing RM sizes and of the specific effects of the surfactant head group.…”

Section: Introductionmentioning

confidence: 99%

On the Structural and Dynamical Properties of DOPC Reverse Micelles

et al. 2016

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The structure and dynamics of phospholipid reverse micelles are studied by molecular dynamics. We report all-atom unconstrained simulations of 1,2-dioleoyl-sn-phosphatidylcholine (DOPC) reverse micelles in benzene of increasing sizes, with water-to-surfactant number ratios ranging from W = 1 to 16. The aggregation number, i.e., the number of DOPC molecules per reverse micelle, is determined to fit experimental light-scattering measurements of the reverse micelle diameter. The simulated reverse micelles are found to be approximately spherical. Larger reverse micelles (W > 4) exhibit a layered structure with a water core and the hydration structure of DOPC phosphate head groups is similar to that found in phospholipid membranes. In contrast, the structure of smaller reverse micelles (W ≤ 4) cannot be described as a series of concentric layers successively containing water, surfactant head groups, and surfactant tails, and the head groups are only partly hydrated and frequently present in the core. The dynamics of water molecules within the phospholipid reverse micelles slow down as the reverse micelle size decreases, in agreement with prior studies on AOT and Igepal reverse micelles. However, the average water reorientation dynamics in DOPC reverse micelles is found to be much slower than in AOT and Igepal reverse micelles with the same W ratio. This is explained by the smaller water pool and by the stronger interactions between water and the charged head groups, as confirmed by the red-shift of the computed infrared line shape with decreasing W.

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Section: Introductionmentioning

confidence: 99%

On the Structural and Dynamical Properties of DOPC Reverse Micelles

et al. 2016

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“…In order to explore a possible membrane organization of the enzyme, we have examined ACE from bovine lung in the reversemicelle system (Kost et al, 1994. The reverse micelle is one of many models thought to have properties resembling more closely the biological cellular environment than the traditional dilute-solution biochemical reaction system (Montal, 1984;Martinek et al, 1989). In these systems, proteins are incorporated into the polar intramicellar spaces and are protected by a monomolecular cover of hydrated surfactant against action of organic solvent.…”

Section: Introductionmentioning

confidence: 99%

New feature of angiotensin‐converting enzyme: carbohydrate‐recognizing domain

et al. 2000

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Self carbohydrate-mediated dimerization of glycoprotein angiotensin-converting enzyme (ACE) was demonstrated. The dimerization was studied in the reverse micelle experimental system as a model of biomembrane situation. Asialo-ACE or agalacto-ACE was able to form a dimer, whereas deglycosylated ACE and sequentially desialylated and degalactosylated ACE failed to dimerize. ACE-ACE interaction was competitively inhibited by Neu5Ac- or Gal-terminated saccharides. The results have allowed us to propose the existence of carbohydrate-recognizing domain (CRD) on ACE molecule. The structural requirements of this CRD were estimated based on the ability of saccharides to inhibit ACE dimerization. The most effective monosaccharides with equal inhibition potencies were shown to be galactose (as GalbetaOMe) and N-acetylneuraminic acid (as Neu5AcalphaOMe). Among oligosaccharides, the most effective ones were found to be 3'SiaLac and, especially, the whole pool of ACE oligosaccharide chains and biantennae complex oligosaccharide chains of other glycoproteins. Bovine and human ACEs were shown to be similar in terms of recognition of carbohydrates.

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“…It should be emphasized that membrane proteins tend to build up supramolecular structures as homo-and heterocomplexes. The reverse micelle is one of many models thought to have properties resembling more closely the biological cellular environment than the traditional dilute-solution biochemical reaction system (Montal, 1984;Martinek et al, 1989). The reverse micelle is one of many models thought to have properties resembling more closely the biological cellular environment than the traditional dilute-solution biochemical reaction system (Montal, 1984;Martinek et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

New feature of angiotensin-converting enzyme: carbohydrate-recognizing domain

et al. 2000

View full text Add to dashboard Cite

Self carbohydrate‐mediated dimerization of glycoprotein angiotensin‐converting enzyme (ACE) was demonstrated. The dimerization was studied in the reverse micelle experimental system as a model of biomembrane situation. Asialo‐ACE or agalacto‐ACE was able to form a dimer, whereas deglycosylated ACE and sequentially desialylated and degalactosylated ACE failed to dimerize. ACE–ACE interaction was competitively inhibited by Neu5Ac‐ or Gal‐terminated saccharides. The results have allowed us to propose the existence of carbohydrate‐recognizing domain (CRD) on ACE molecule. The structural requirements of this CRD were estimated based on the ability of saccharides to inhibit ACE dimerization. The most effective monosaccharides with equal inhibition potencies were shown to be galactose (as GalβOMe) and N‐acetylneuraminic acid (as Neu5AcαOMe). Among oligosaccharides, the most effective ones were found to be 3′SiaLac and, especially, the whole pool of ACE oligosaccharide chains and biantennae complex oligosaccharide chains of other glycoproteins. Bovine and human ACEs were shown to be similar in terms of recognition of carbohydrates. Copyright © 2000 John Wiley & Sons, Ltd.

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On the Structure, Dynamics and Possible Functional Roles of Inverted Micelles in Biological Membranes

Cited by 10 publications

References 38 publications

On the Structural and Dynamical Properties of DOPC Reverse Micelles

On the Structural and Dynamical Properties of DOPC Reverse Micelles

New feature of angiotensin‐converting enzyme: carbohydrate‐recognizing domain

New feature of angiotensin-converting enzyme: carbohydrate-recognizing domain

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