References of "Crowet, Jean-Marc"
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See detailGROMPALA: a membrane-implicit modelling method to screen lipid-interacting molecules
Steinhauer, Sven; Crowet, Jean-Marc ULg; Brasseur, Robert ULg et al

in Software and techniques for Bio-molecular modeling (in press)

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See detailInteractions of sugar-based bolaamphiphiles with biomimetic systems of plasma membranes
Nasir, Mehmet Nail ULg; Crowet, Jean-Marc ULg; Lins, Laurence ULg et al

in Biochimie (2016), In Press

Glycolipids constitute a class of molecules with various biological activities. Among them, sugar-based bolaamphiphiles characterized by their biocompatibility, biodegradability and lower toxicity, became ... [more ▼]

Glycolipids constitute a class of molecules with various biological activities. Among them, sugar-based bolaamphiphiles characterized by their biocompatibility, biodegradability and lower toxicity, became interesting for the development of efficient and low cost lipid-based drug delivery systems. Their activity seems to be closely related to their interactions with the lipid components of the plasma membrane of target cells. Despite many works devoted to the chemical synthesis and characterization of sugar-based bolaamphiphiles, their interactions with plasma membrane have not been completely elucidated. In this work, two sugar-based bolaamphiphiles differing only at the level of their sugar residues were chemically synthetized. Their interactions with membranes have been investigated using model membranes containing or not sterol and with in silico approaches. Our findings indicate that the nature of sugar residues has no significant influence for their membrane interacting properties, while the presence of sterol attenuates the interactions of both bolaamphiphiles with the membrane systems. The understanding of this distinct behavior of bolaamphiphiles towards sterol-containing membrane systems could be useful for their applications as drug delivery systems. [less ▲]

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See detailExperimental and in silico approaches to study the interaction of Remorin with plant plasma membrane : specific interaction of the C-term domain with lipids
Deleu, Magali ULg; Nasir, Mehmet Nail ULg; Gronnier, Julien et al

Conference (2015, September 29)

The function of Remorins, a diverse family of plant-specific proteins (1) is far to be fully elucidated. One of them, StREM1.3 (for Solanum tuberosum Remorin from group 1, homolog 3) has been reported to ... [more ▼]

The function of Remorins, a diverse family of plant-specific proteins (1) is far to be fully elucidated. One of them, StREM1.3 (for Solanum tuberosum Remorin from group 1, homolog 3) has been reported to regulate cell-to-cell propagation of the potato virus X (2). It was also shown to be localized to the inner leaflet of plasma membranes (PMs) and along plasmodesmata, bridges connecting neighbor cells essential for cell-to-cell communication in plants (3). The mechanisms driving StREM1.3 association with PM is still an open question. It was shown recently that a domain of 28 residues at the C-terminus of the potato (RemCA) is required and sufficient for anchoring to the PM (4). Here we combined experimental and in silico biophysics to unravel the molecular bases of RemCA membrane binding. Biomimetic membrane models of plant PM such as monolayers and liposomes were used with various biophysical techniques (Langmuir monolayer technique, Fourier-transformed infrared spectroscopy, circular dichroïsm) and modeling tools (home-made methods and molecular dynamics) (5) to answer to three questions: (i) What is the conformation adopted by RemCA within a membrane?, (ii) Is there any membrane lipid specificity in the RemCA-membrane binding? (iii) What is the role of the two different RemCA domains in the interaction? Results show that RemCA displays a preference for plant phosphoinositide and sitosterol-enriched inner leaflet plasma membrane rafts. Within the membrane, the C-terminal and the N-terminal domains adopt a random coil and a -helical conformation respectively. The C-terminal domain acts as a driver to bind RemCA to the membrane while the N-terminal domain stabilizes the peptide at the membrane. Lysine residues have a crucial importance in this interaction. References (1) Raffaele et al., Plant Physiol., 2007, 145: 593–600 (2) Raffaela et al., Plant Cell, 2009, 21: 1541–1555. (3) Maule, Curr. Opin. Plant Biol., 2008, 11: 680–686. (4) Perraki et al., Plant Physiology, 2012, 160 : 624-637. (5) Deleu et al., Biochim. Biophys. Acta – Biomembranes, 2014, 1838 : 3171-3190. [less ▲]

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See detailSurfactin: a receptor-independent bacterial elicitor of plant immunity?
Luzuriaga Loaiza, Walter ULg; Legras, Aurelien; Crowet, Jean-Marc ULg et al

Poster (2015, May 13)

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See detailModeling of the cyclic lipodepsipeptide Pseudodesmin A self-assembly through molecular dynamic simulations
Crowet, Jean-Marc ULg; Sinnaeve, Davy; Fehér, Krisztina et al

Conference (2014, September 30)

The self-assembly of short peptides into supramolecular structures represents an active field of research with potential applications, ranging from material sciences to medicine. Pseudodesmine A is a ... [more ▼]

The self-assembly of short peptides into supramolecular structures represents an active field of research with potential applications, ranging from material sciences to medicine. Pseudodesmine A is a cyclic lipodepsipeptide of nine residues which presents a moderate antibacterial activity and whose structure has been resolved by X-ray and NMR. In acetonitrile, Pseudodesmine A is monomeric while in chloroform, it has the same structure but assembles in a supramolecular complex. This structure could associate with membranes and be responsible for the biological activity of the peptide. Comparison of NMR data in the two solvents has given indications on the intermolecular contacts that arise in chloroform and a model for the self-association was proposed. To study in more details this assembly, molecular dynamics simulations have been carried on. The resultswere compared with detailed information given by NMR, regarding the dimensions of the assembly and the orientation of the individual peptide building blocks inside the supramolecular assembly. In acetonitrile, the simulations show that the peptide has transient interactions while in chloroform, interactions between monomers are always observed. In agreement with NMR, these interactions arise mainly between the backbone protons of the LEU1 and the GLN2, the GLN2 sidechain and the loop located on the opposite end of the monomer structure. From 10 simulations of dimerization, hydrogen bonds were followed and specific interaction patterns were identified regarding the hydrogen bonds formed. Peptide interactions are mainly described by 13 interaction patterns characterized by 2 to 4 hydrogen bonds. In dimers, the peptides can have a linear, a perpendicular or a side by side configuration. From the linear dimer, it is possible to reconstruct filaments and, by combining a linear and a lateral dimer, it is possible to build fibrils with multifilaments, as found in the NMR-derived model. Two self-consistent supramolecular models can be built from dimers and they present a very good correlation with NMR data regarding the supramolecular organization. Besides, the perpendicular dimer can gives peptide rings that can also explain the potential ability of this peptide to form ion pores in membranes. [less ▲]

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See detailModeling of the cyclic lipodepsipeptide Pseudodesmin A self-assembly through molecular dynamic simulations
Crowet, Jean-Marc ULg; Sinnaeve, Davy; Fehér, Krisztina et al

Poster (2014, August 21)

The self-assembly of short peptides into supramolecular structures represents an active field of research with potential applications, ranging from material sciences to medicine. Pseudodesmine A is a ... [more ▼]

The self-assembly of short peptides into supramolecular structures represents an active field of research with potential applications, ranging from material sciences to medicine. Pseudodesmine A is a cyclic lipodepsipeptide of nine residues which presents a moderate antibacterial activity and whose structure has been resolved by X-ray and NMR. In acetonitrile, Pseudodesmine A is monomeric while in chloroform, it has the same structure but assembles in a supramolecular complex. This structure could associate with membranes and be responsible for the biological activity of the peptide. Comparison of NMR data in the two solvents has given indications on the intermolecular contacts that arise in chloroform and a model for the self-association was proposed. To study in more details this assembly, molecular dynamics simulations have been carried on. The resultswere compared with detailed information given by NMR, regarding the dimensions of the assembly and the orientation of the individual peptide building blocks inside the supramolecular assembly. In acetonitrile, the simulations show that the peptide has transient interactions while in chloroform, interactions between monomers are always observed. In agreement with NMR, these interactions arise mainly between the backbone protons of the LEU1 and the GLN2, the GLN2 sidechain and the loop located on the opposite end of the monomer structure. From 10 simulations of dimerization, hydrogen bonds were followed and specific interaction patterns were identified regarding the hydrogen bonds formed. Peptide interactions are mainly described by 13 interaction patterns characterized by 2 to 4 hydrogen bonds. In dimers, the peptides can have a linear, a perpendicular or a side by side configuration. From the linear dimer, it is possible to reconstruct filaments and, by combining a linear and a lateral dimer, it is possible to build fibrils with multifilaments, as found in the NMR-derived model. Two self-consistent supramolecular models can be built from dimers and they present a very good correlation with NMR data regarding the supramolecular organization. Besides, the perpendicular dimer can gives peptide rings that can also explain the potential ability of this peptide to form ion pores in membranes. [less ▲]

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See detailModeling of the cyclic lipodepsipeptide Pseudodesmin A self-assembly through molecular dynamic simulations
Crowet, Jean-Marc ULg; Sinnaeve, Davy; Fehér, Krisztina et al

Conference (2014, August 20)

The self-assembly of short peptides into supramolecular structures represents an active field of research with potential applications, ranging from material sciences to medicine. Pseudodesmine A is a ... [more ▼]

The self-assembly of short peptides into supramolecular structures represents an active field of research with potential applications, ranging from material sciences to medicine. Pseudodesmine A is a cyclic lipodepsipeptide of nine residues which presents a moderate antibacterial activity and whose structure has been resolved by X-ray and NMR. In acetonitrile, Pseudodesmine A is monomeric while in chloroform, it has the same structure but assembles in a supramolecular complex. This structure could associate with membranes and be responsible for the biological activity of the peptide. Comparison of NMR data in the two solvents has given indications on the intermolecular contacts that arise in chloroform and a model for the self-association was proposed. To study in more details this assembly, molecular dynamics simulations have been carried on. The resultswere compared with detailed information given by NMR, regarding the dimensions of the assembly and the orientation of the individual peptide building blocks inside the supramolecular assembly. In acetonitrile, the simulations show that the peptide has transient interactions while in chloroform, interactions between monomers are always observed. In agreement with NMR, these interactions arise mainly between the backbone protons of the LEU1 and the GLN2, the GLN2 sidechain and the loop located on the opposite end of the monomer structure. From 10 simulations of dimerization, hydrogen bonds were followed and specific interaction patterns were identified regarding the hydrogen bonds formed. Peptide interactions are mainly described by 13 interaction patterns characterized by 2 to 4 hydrogen bonds. In dimers, the peptides can have a linear, a perpendicular or a side by side configuration. From the linear dimer, it is possible to reconstruct filaments and, by combining a linear and a lateral dimer, it is possible to build fibrils with multifilaments, as found in the NMR-derived model. Two self-consistent supramolecular models can be built from dimers and they present a very good correlation with NMR data regarding the supramolecular organization. Besides, the perpendicular dimer can gives peptide rings that can also explain the potential ability of this peptide to form ion pores in membranes. [less ▲]

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See detailMembrane interactions of cyclic lipodepsipeptides from the viscosin group
Geudens, Niels; Feher, Krisztina; De Vleeschouwer et al

Poster (2014, June)

Detailed reference viewed: 15 (4 ULg)
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See detailMolecular dynamic simulation of the cyclic lipodepsipeptide Pseudodesmin A self-assembly
Crowet, Jean-Marc ULg; Sinnaeve, Davy; Fehér, Krisztina et al

Conference (2014, February 10)

Pseudodesmine A is a cyclic lipodepsipeptide of nine residues which presents a moderate antibacterial activity and whose structure has been resolved by X-ray and NMR1,2. In acetonitrile, Pseudodesmine A ... [more ▼]

Pseudodesmine A is a cyclic lipodepsipeptide of nine residues which presents a moderate antibacterial activity and whose structure has been resolved by X-ray and NMR1,2. In acetonitrile, Pseudodesmine A is monomeric while in chloroform it has the same structure but assemble in a supramolecular complex. This structure could associate with membranes and be responsible of the biological activity of this peptide. Comparison of the NMR data between the two solvents has given indications on the intermolecular contacts that arise in chloroform and a model for the self association was proposed2,3. To study in more details this assembly, molecular dynamics have been carried on. In acetonitrile, the peptide show transient interactions while in chlorofom interactions between monomers was always observed. As stated in Sinnaeve et al. in 2009, these interactions arise mainly between the backbone protons of the LEU1 and the GLN2, the GLN2 sidechain and the loop located on the opposite end of the monomer structure. From 10 simulations of dimerization, hydrogen bonds were followed and specific interaction patterns were identified regarding the hydrogen bonds formed. The peptide interactions are mainly described by 13 interaction patterns; 8 with the peptides in a linear configuration, 1 perpendicular and 4 with peptides side by side. The patterns are characterized by 2 to 4 hydrogen bonds. From the linear dimer, it is possible to reconstruct filaments and, by combining a linear and a lateral dimer, it is possible to build fibrils with multi filaments, as expected in the NMR derived model. Besides, the perpendicular dimer can gives peptide rings that can also explain the potential ability of this peptide to form ion pores in membranes. 1. Sinnaeve, D., Michaux, C., Van hemel, J., Vandenkerckhove, J., Peys, E., Borremans, F. a. M., Sas, B., Wouters, J. and Martins, J. C. Tetrahedron 2009, 65, 4173–4181. 2. Sinnaeve, D., Hendrickx, P. M. S., Van Hemel, J., Peys, E., Kieffer, B. and Martins, J. C. Chemistry (Weinheim an der Bergstrasse, Germany) 2009, 15, 12653–62. 3. Sinnaeve, D., Delsuc, M.-A., Martins, J. C. and Kieffer, B. Chemical Science 2012, 3, 1284. [less ▲]

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See detailInteractions between new phenolic glycolipids and model membrane
Sainvitu, Pauline ULg; Nasir, Mehmet Nail ULg; Crowet, Jean-Marc ULg et al

Poster (2014, February 07)

Model membrane based on phospholipids (PL) layers are useful to mimic properties of plasma membranes. The interactions between new synthesized phenolic glycolipids (PGL) and biological membrane are ... [more ▼]

Model membrane based on phospholipids (PL) layers are useful to mimic properties of plasma membranes. The interactions between new synthesized phenolic glycolipids (PGL) and biological membrane are crucial to determine their potential as drug candidates and their cytotoxicity . [less ▲]

Detailed reference viewed: 51 (5 ULg)