scholarly journals Asymmetric Synthesis and Binding Study of New Long-Chain HPA-12 Analogues as Potent Ligands of the Ceramide Transfer Protein CERT

2016 ◽  
Vol 22 (19) ◽  
pp. 6676-6686 ◽  
Author(s):  
Andrej Ďuriš ◽  
Adam Daïch ◽  
Cécile Santos ◽  
Laurence Fleury ◽  
Frédéric Ausseil ◽  
...  
Keyword(s):  
Asymmetric Synthesis ◽  
Binding Study ◽  
Transfer Protein ◽  
Long Chain

Asymmetric Synthesis of the Cholesteryl Ester Transfer Protein Inhibitor Torcetrapib

2006 ◽  
Vol 10 (3) ◽  
pp. 472-480 ◽  
Author(s):  
David B. Damon ◽  
Robert W. Dugger ◽  
Stephen E. Hubbs ◽  
Jill M. Scott ◽  
Robert W. Scott
Keyword(s):  
Cholesteryl Ester ◽  
Asymmetric Synthesis ◽  
Cholesteryl Ester Transfer Protein ◽  
Protein Inhibitor ◽  
Transfer Protein

scholarly journals A phospholipid transfer protein that binds long-chain fatty acids

FEBS Letters ◽  
1985 ◽  
Vol 180 (1) ◽  
pp. 29-32 ◽  
Author(s):  
Jutta Rickers ◽  
Friedrich Spener ◽  
Jean-Claude Kader
Keyword(s):  
Fatty Acids ◽  
Phospholipid Transfer Protein ◽  
Long Chain Fatty Acids ◽  
Transfer Protein ◽  
Phospholipid Transfer ◽  
Long Chain ◽  
Chain Fatty Acids

Efficient Asymmetric Synthesis of Long-Chain Polyketides Containing up to Ten Contiguous Stereogenic Centres by Double Chain Elongation

2011 ◽  
Vol 2011 (18) ◽  
pp. 3317-3328 ◽  
Author(s):  
Maris Turks ◽  
Kelly A. Fairweather ◽  
Rosario Scopelliti ◽  
Pierre Vogel
Keyword(s):  
Asymmetric Synthesis ◽  
Chain Elongation ◽  
Double Chain ◽  
Long Chain

Evidence for an ATP-independent long-chain phosphatidylcholine translocator in hepatocyte membranes

1997 ◽  
Vol 273 (6) ◽  
pp. G1312-G1319 ◽  
Author(s):  
Michael Fuchs ◽  
Martin C. Carey ◽  
David E. Cohen
Keyword(s):  
Membrane Proteins ◽  
Xenopus Laevis ◽  
Gene Product ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Heat Denaturation ◽  
Xenopus Laevis Oocytes ◽  
Erythrocyte Ghosts ◽  
Transfer Protein ◽  
Long Chain

Transport of phosphatidylcholine (PC) molecules across canalicular plasma membranes of the liver is essential for their secretion into bile. To test for evidence of protein-mediated translocation of natural long-chain PCs, we investigated whether hepatocyte membrane subfractions reconstituted into proteoliposomes promoted transmembrane translocation of radiolabeled PCs. Translocation of PC molecules in proteoliposomes was measured by an assay that employed multilamellar acceptor vesicles and the specific PC transfer protein purified from liver. As inferred from the percentage of radiolabel removed from proteoliposomes, facilitated PC translocation occurred in microsomes and canalicular and basolateral plasma membranes from rat liver but not in erythrocyte ghosts, microsomes, homogenates of COS and H35 cells, or Xenopus laevis oocytes. Heat denaturation in the presence of 2-mercaptoethanol and Pronase digestion of solubilized membrane proteins inhibited translocation. In contrast to the mdr2 gene product (Mdr2), which promotes ATP-dependent, verapamil-inhibitable PC translocation, ATP did not enhance and verapamil failed to block PC translocation. These data support the possibility that an ATP-independent PC translocator, possibly distinct from Mdr2, may be present in hepatocyte canalicular plasma membranes.

scholarly journals High-affinity binding of very-long-chain fatty acyl-CoA esters to the peroxisomal non-specific lipid-transfer protein (sterol carrier protein-2)

1999 ◽  
Vol 339 (1) ◽  
pp. 193-199 ◽  
Author(s):  
Tobias B. DANSEN ◽  
Jan WESTERMAN ◽  
Fred S. WOUTERS ◽  
Ronald J. A. WANDERS ◽  
Arie van HOEK ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Lipid Transfer Protein ◽  
Fatty Acyl ◽  
Lipid Binding ◽  
Tryptophan Residue ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Specific Lipid ◽  
Long Chain ◽  
Lipid Binding Site

Binding of fluorescent fatty acids to bovine liver non-specific lipid-transfer protein (nsL-TP) was assessed by measuring fluorescence resonance energy transfer (FRET) between the single tryptophan residue of nsL-TP and the fluorophore. Upon addition of pyrene dodecanoic acid (Pyr-C12) and cis-parinaric acid to nsL-TP, FRET was observed indicating that these fatty acids were accommodated in the lipid binding site closely positioned to the tryptophan residue. Substantial binding was observed only when these fatty acids were presented in the monomeric form complexed to β-cyclodextrin. As shown by time-resolved fluorescence measurements, translocation of Pyr-C12 from the Pyr-C12–β-cyclodextrin complex to nsL-TP changed dramatically the direct molecular environment of the pyrene moiety: i.e. the fluorescence lifetime of the directly excited pyrene increased at least by 25% and a distinct rotational correlation time of 7 ns was observed. In order to evaluate the affinity of nsL-TP for intermediates of the β-oxidation pathway, a binding assay was developed based on the ability of fatty acyl derivatives to displace Pyr-C12 from the lipid binding site as reflected by the reduction of FRET. Hexadecanoyl-CoA and 2-hexadecenoyl-CoA were found to bind readily to nsL-TP, whereas 3-hydroxyhexadecanoyl-CoA and 3-ketohexadecanoyl-CoA bound poorly. The highest affinities were observed for the very-long-chain fatty acyl-CoA esters (24:0-CoA, 26:0-CoA) and their enoyl derivatives (24:1-CoA, 26:1-CoA). Binding of non-esterified hexadecanoic acid and tetracosanoic acid (24:0) was negligible.

Asymmetric synthesis of new chiral long chain alcohols

2010 ◽  
Vol 21 (24) ◽  
pp. 2981-2987 ◽  
Author(s):  
Tülay Yıldız ◽  
Ayşe Yusufoğlu
Keyword(s):  
Asymmetric Synthesis ◽  
Long Chain
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