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See detailModeling of non-covalent complexes of the cell-penetrating peptide CADY and its siRNA cargo
Crowet, Jean-Marc ULg; Lins, Laurence ULg; Deshayes, Sébastien et al

in European Biophysics Journal [=EBJ] (2013), 42(S1), 63

CADY is a cell-penetrating peptide spontaneously making non-covalent complexes with short interfering RNAs (siRNAs) in water. Neither the structure of CADY nor that of the complexes is resolved. We have ... [more ▼]

CADY is a cell-penetrating peptide spontaneously making non-covalent complexes with short interfering RNAs (siRNAs) in water. Neither the structure of CADY nor that of the complexes is resolved. We have calculated and analyzed 3D models of CADY and of the non-covalent CADY–siRNA complexes in order to understand their formation and stabilization. Data from the ab initio calculations and molecular dynamics support that, in agreement with the experimental data, CADY is a polymorphic peptide partly helical. We calculated and compared several complexes with peptide/siRNA ratios of up to 40. The initial binding of CADYs is essentially due to the electrostatic interactions of the arginines with siRNA phosphates. Due to a repetitive arginine motif (XLWR(K)), CADYs can adopt multiple positions at the siRNA surface. Nevertheless, several complex properties are common: an average of 14 ± 1 CADYs is required to saturate a siRNA. The 40 CADYs/siRNA that is the optimal ratio for vector stability always corresponds to two layers of CADYs per siRNA and the peptide cage is stabilized by hydrophobic CADY–CADY contacts. The analysis demonstrates that the hydrophobicity, the positive charges and the polymorphism of CADY are mandatory to make stable the CADY–siRNA complexes. [less ▲]

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See detailInteresterification of rapeseed oil with anhydrous milk fat and its stearin fraction. II. Modifications of melting properties
Giet, Jean-Michel ULg; Aguedo, Mario ULg; Hanon, Emilien ULg et al

in GCIRC Bulletin (2009), 25

Chemical and/or physical modification of oils and fats are commonly used by food industry to widen their range of applications (1,2). Lipase-catalysed interesterification of anhydrous milk fat (AMF) and ... [more ▼]

Chemical and/or physical modification of oils and fats are commonly used by food industry to widen their range of applications (1,2). Lipase-catalysed interesterification of anhydrous milk fat (AMF) and various vegetable oils is now a well documented procedure (3-7). The purpose of this technique is to produce original structured fats with properties different from a simple blending, that may be used as spreads or introduced into pastry. The new fats contain higher amounts of polyunsaturated fatty acids (PUFA) than butter, which provides health benefits (8,9). To our knowledge only a few authors associated AMF fractionation with blending and interesterification (10,11), although this combination may be used to increase the ratio of vegetable oil in blends and thus the PUFA content of the product. The compositional changes occurring during the lipase-catalysed interesterification of AMF/rapeseed oil (RO) and AMF stearin fraction (AMFSF)/RO blends were described in the first part of this study. In the present and second part are reported the resulting changes in physical properties, especially the melting behaviour through solid fat content (SFC), dropping point (DP) and fusion profiles by differential scanning calorimetry (DSC). [less ▲]

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See detailEnzymatic interesterification of anhydrous milk fat with rapeseed and/or linseed oil: oxidative stability
Giet, Jean-Michel ULg; Aguedo, Mario ULg; Danthine, Sabine ULg et al

in Journal of Agricultural and Food Chemistry (2009), 57(15), 6787-6794

Blends of anhydrous milkfat (AMF) and linseed oil (70/30), and AMF, rapeseed oil (RO) and linseed oil (LO), 70/20/10, were submitted to enzymatic interesterification. The oxidative stability of the blends ... [more ▼]

Blends of anhydrous milkfat (AMF) and linseed oil (70/30), and AMF, rapeseed oil (RO) and linseed oil (LO), 70/20/10, were submitted to enzymatic interesterification. The oxidative stability of the blends, the interesterified (IE) blends and IE blends with 50 ppm -tocopherol added as antioxidant were studied. Samples were stored in open flasks at 60°C, 25°C and 4°C, and periodically submitted to peroxide, p-anisidine, TBA value determination and UV measurement at 232 and 268 nm. The analysis of volatile compounds was carried out by SPME for the samples stored at 60°C. Peroxides appeared to be the only significant oxidation products after 12 weeks storage at 4°C. As expected, the binary blends (BB) were more sensitive to oxidation than the ternary blends (TB). The BB were associated with increased volatile emission compared to TB. Interesterification led to variable effects on the oxidation of fat mixtures, depending on composition and temperature (beneficial effect on BB, at both 25°C and 60°C, and a rather neutral effect on TB). The IE blends exhibited higher volatile release prior to ageing. A pro-oxidant effect of -tocopherol addition was observed at 25°C on both BB and TB. At 60°C, an antioxidant effect was observed on TB. [less ▲]

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See detailEnrichment of anhydrous milk fat in polyunsaturated fatty acid residues from linseed and rapeseed oils through enzymatic interesterification
Aguedo, Mario ULg; Hanon, EMILIEN ULg; Danthine, Sabine ULg et al

in Journal of Agricultural and Food Chemistry (2008), 56(5), 1757-1765

Lipozyme TL IM was used in a solvent-free batch and microaqueous system for enzymatic interesterification of anhydrous milkfat (AMF) with linseed oil (LO) in binary blends and with rapeseed oil (RO) in ... [more ▼]

Lipozyme TL IM was used in a solvent-free batch and microaqueous system for enzymatic interesterification of anhydrous milkfat (AMF) with linseed oil (LO) in binary blends and with rapeseed oil (RO) in one ternary blend. The aim was to obtain and characterize physicochemically fats enriched with unsaturated C-18 fatty acids (oleic, linoleic, and, especially, linolenic acids) from natural vegetable oils. Binary blends of AMF/LO 100/0, 90/10, 80/20, 70/30, and 60/40 (w/w) were interesterified. The change in triacylglycerol (TAG) profiles showed that quasi-equilibrium conditions were reached after 4-6 h of reaction. Free fatty acid contents < 1%. The decrease in solid fat content and in dropping point temperature obtained with increasing content of LO and interesterification resulted in good plastic properties for the products originating from the blends 70/30 and 60/40. This was confirmed by textural measurements. Melting profiles determined by differential scanning calorimetry showed complete disappearance of low-melting TAGs from LO and the formation of intermediary species with a lower melting temperature. Oxidative stability of the interesterified products was diminished with increasing LO content, resulting in low oxidation induction times. A ternary blend composed of AMF/RO/LO 70/20/10 gave satisfactory rheological and oxidative properties, fulfilling the requirements for a marketable spread and, moreover, offering increased potential health benefits due to the enriched content in polyunsatured fatty acid residues. [less ▲]

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See detailFunctional analysis of the cell division protein FtsW of Escherichia coli
Pastoret, Soumya; Fraipont, Claudine ULg; den Blaauwen, Tanneke et al

in Journal of Bacteriology (2004), 186(24), 8370-8379

Site-directed mutagenesis experiments combined with fluorescence microscopy shed light on the role of Escherichia coli FtsW, a membrane protein belonging to the SEDS family that is involved in ... [more ▼]

Site-directed mutagenesis experiments combined with fluorescence microscopy shed light on the role of Escherichia coli FtsW, a membrane protein belonging to the SEDS family that is involved in peptidoglycan assembly during cell elongation, division, and sporulation. This essential cell division protein has 10 transmembrane segments (TMSs). It is a late recruit to the division site and is required for subsequent recruitment of penicillin-binding protein 3 (PBP3) catalyzing peptide cross-linking. The results allow identification of several domains of the protein with distinct functions. The localization of PBP3 to the septum was found to be dependent on the periplasmic loop located between TMSs 9 and 10. The E240-A249 amphiphilic peptide in the periplasmic loop between TMSs 7 and 8 appears to be a key element in the functioning of FtsW in the septal peptidoglycan assembly machineries. The intracellular loop (containing the R166-FI78 amphiphilic peptide) between TMSs 4 and 5 and Gly 311 in TMS 8 are important components of the amino acid sequence-folding information. [less ▲]

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See detailStudy of the potential role of tilted peptides in transconformation: Theoritical analysis of amyloidogenic proteins
Crowet, Jean-Marc ULg; Brasseur, Robert ULg; Thomas, Annick et al

Poster (2003, May 23)

Amyloidogenic proteins are of interest in the study of transconformational processes because they undergo a major conformational change leading to amyloid fibrils formation by a self-assembly of their ... [more ▼]

Amyloidogenic proteins are of interest in the study of transconformational processes because they undergo a major conformational change leading to amyloid fibrils formation by a self-assembly of their misfolded form.  Amyloid fibrils are implied in several diseases such as Alzheimer, Parkinson or Creutzfeldt-Jakob diseases. At a structural point of view they have varying lengths up to few micrometers, they are unbranched and the individual β strands are oriented perpendicular to the long axis of the fibril. Moreover, the conformational changes induce an increase in the β content. However little is known about the mechanisms of transconformation, the subsequent aggregation and the toxicity of these proteins. Study of these misfolded proteins, and particularly the study of their conformation, is difficult due to their high tendency to aggregate in solution.  Regarding the transconformational mechanisms, it’s interesting to study the potential role of tilted peptides because they possess several properties that could be involved in this process. They can adopt  or β conformation depending on the environment and when helical they can destabilize the hydrophilic/hydrophobic interface of an organised system. They were notably found in the domain undergoing transconformation in the A protein (Alzheimer’s disease) and in PrP (prion diseases). They could have an important role in the first step of the transconformational process ; their destabilizing properties could also be implied in the toxicity of these proteins.  The aim of this study is to analyse the sequence of amyloidogenic proteins undergoing  to  transition, looking for tilted peptides. From their primary sequence, Eisenberg’s hydrophobic moment plot, hydrophobic cluster analysis, Jähnig’s plot and several methods for the prediction of secondary structure have been carried out. Fragments corresponding to potential tilted peptides following different criteria (mean of hydrophobicity, length, …) were 3D built and their insertion into a simplified bilayer was simulated using the IMPALA method. A detailed study of the literature should provide more information about the particular properties of these sequences and the existence of these tilted peptides must be demonstrated by experimental techniques. The tilted fragment from -synuclein (Parkinson’s disease) is under current investigations. [less ▲]

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