Publications
2013
Schaeffer Evelyne, Dehuyser Laure, Sigwalt David, Flacher Vincent, Bernacchi Serena, Chaloin Olivier, Remy Jean-Serge, Mueller Christopher G, Baati Rachid, Wagner Alain
Dynamic micelles of mannoside glycolipids are more efficient than polymers for inhibiting HIV-1 trans-infection Article de journal
Dans: Bioconjugate Chemistry, vol. 24, no. 11, p. 1813–1823, 2013, ISSN: 1520-4812.
Résumé | Liens | BibTeX | Étiquettes: Anti-HIV Agents, Calcium, Cells, Chemistry, Cultured, Dendritic Cells, Dose-Response Relationship, Drug, Electron, fluorescence, Glycolipids, HIV, HIV Infections, HIV-1, Human, Humans, immunodeficiency, immunopathology, inhibition, LECTIN, Lectins, lipid, Mannosides, Micelles, Microbial Sensitivity Tests, Microscopy, Models, Molecular, Molecular Structure, Polymers, prophylaxis, Spectrometry, Structure-Activity Relationship, Surface Plasmon Resonance, target, Team-Mueller, Thermodynamics, Transmission, virus
@article{schaeffer_dynamic_2013,
title = {Dynamic micelles of mannoside glycolipids are more efficient than polymers for inhibiting HIV-1 trans-infection},
author = {Evelyne Schaeffer and Laure Dehuyser and David Sigwalt and Vincent Flacher and Serena Bernacchi and Olivier Chaloin and Jean-Serge Remy and Christopher G Mueller and Rachid Baati and Alain Wagner},
doi = {10.1021/bc4000806},
issn = {1520-4812},
year = {2013},
date = {2013-11-01},
journal = {Bioconjugate Chemistry},
volume = {24},
number = {11},
pages = {1813--1823},
abstract = {Mannoside glycolipid conjugates are able to inhibit human immunodeficiency virus type 1 (HIV-1) trans-infection mediated by human dendritic cells (DCs). The conjugates are formed by three building blocks: a linear or branched mannose head, a hydrophilic linker, and a 24-carbon lipid chain. We have shown that, even as single molecules, these compounds efficiently target mannose-binding lectins, such as DC-specific ICAM-3-grabbing nonintegrin (DC-SIGN) important for HIV-1 transmission. With the goal to optimize their inhibitory activity by supramolecular structure formation, we have compared saturated and unsaturated conjugates, as single molecules, self-assemblies of dynamic micelles, and photopolymerized cross-linked polymers. Surface plasmon resonance showed that, unexpectedly, polymers of trivalent conjugates did not display a higher binding affinity for DC-SIGN than single molecules. Interactions on a chip or in solution were independent of calcium; however, binding to DCs was inhibited by a calcium chelator. Moreover, HIV-1 trans-infection was mostly inhibited by dynamic micelles and not by rigid polymers. The inhibition data revealed a clear correlation between the structure and molecular assembly of a conjugate and its biological antiviral activity. We present an interaction model between DC-SIGN and conjugates-either single molecules, micelles, or polymers-that highlights that the most effective interactions by dynamic micelles involve both mannose heads and lipid chains. Our data reveal that trivalent glycolipid conjugates display the highest microbicide potential for HIV prophylaxis, as dynamic micelles conjugates and not as rigid polymers.},
keywords = {Anti-HIV Agents, Calcium, Cells, Chemistry, Cultured, Dendritic Cells, Dose-Response Relationship, Drug, Electron, fluorescence, Glycolipids, HIV, HIV Infections, HIV-1, Human, Humans, immunodeficiency, immunopathology, inhibition, LECTIN, Lectins, lipid, Mannosides, Micelles, Microbial Sensitivity Tests, Microscopy, Models, Molecular, Molecular Structure, Polymers, prophylaxis, Spectrometry, Structure-Activity Relationship, Surface Plasmon Resonance, target, Team-Mueller, Thermodynamics, Transmission, virus},
pubstate = {published},
tppubtype = {article}
}
2003
Salah R. Ben, Zouari N., Reinbolt J., Mejdoub H.
Purification of turkey pancreatic phospholipase A2 Article de journal
Dans: Biosci Biotechnol Biochem, vol. 67, no. 10, p. 2139-44, 2003, (0916-8451 Journal Article).
Résumé | BibTeX | Étiquettes: *Turkeys, &, A/*isolation, Acid, acids, Amino, Ammonium, and, Animals, Bile, Calcium, Chromatography, Concentration, Data, Hydrogen-Ion, Molecular, Pancreas/*enzymology, Phospholipases, purification, Salts, Sequence, Sulfate, Temperature, Weight
@article{,
title = {Purification of turkey pancreatic phospholipase A2},
author = { R. Ben Salah and N. Zouari and J. Reinbolt and H. Mejdoub},
year = {2003},
date = {2003-01-01},
journal = {Biosci Biotechnol Biochem},
volume = {67},
number = {10},
pages = {2139-44},
abstract = {Turkey pancreatic phospholipase (TPP) has been purified from delipidated pancreases. The purification included ammonium sulfate fractionation, acidic (pH 5) treatment, followed by sequencial column chromatographies on DEAE-cellulose, Sephadex G-75, and reverse phase high pressure liquid chromatography. The purified enzyme was found to be a monomeric protein with molecular mass of 14 kDa. The optimal activity was measured at pH 8 and 37 degrees C using egg yolk emulsion as substrate. Our results show that the enzyme (TPP) was not stable for 1 h at 60 degrees C, and that bile salt and Ca2+ were required for the expression of the purified enzyme. The sequence of the N-terminal amino acids of the purified enzyme shows a very close similarity between TPP and all other known pancreatic phospholipases.},
note = {0916-8451
Journal Article},
keywords = {*Turkeys, &, A/*isolation, Acid, acids, Amino, Ammonium, and, Animals, Bile, Calcium, Chromatography, Concentration, Data, Hydrogen-Ion, Molecular, Pancreas/*enzymology, Phospholipases, purification, Salts, Sequence, Sulfate, Temperature, Weight},
pubstate = {published},
tppubtype = {article}
}