64701-47-9Relevant academic research and scientific papers
New Fluorescence from Molecular Aggregates of 10-(1-pyrenyl)decanoic Acid
Itaya, Akira,Kawamura, Tsuneo,Masuhara, Hiroshi,Taniguchi, Yoshio,Mitsuya, Munehisa,et al.
, p. 1541 - 1544 (1986)
In addition to the normal monomer and excimer fluorescence, vacuum-deposited, cast and their laser-irradiated films of 10-(1-pyrenyl)decanoic acid showed three kinds of fluorescence bands.Similar new fluorescence bands were also observed in its aqueous solution.These emissions were due to meta-stable aggregates of pyrenyl chromophores whose structures were ascribed to molecular interactions operating during the processes of film preparation.
Synthesis of a novel fluorescent ceramide analogue and its use in the characterization of recombinant ceramidase from Pseudomonas aeruginosa PA01
Nieuwenhuizen, Willem F,Leeuwen, Sander van,Goetz, Friedrich,Egmond, Maarten R
, p. 181 - 191 (2007/10/03)
Ceramidase (CDase) hydrolyses the N-acyl linkage of the sphingolipid ceramide. We synthesized the non-fluorescent ceramide analogue (4E,2S,3R)-2-N-(10-pyrenedecanoyl)-1,3,17-trihydroxy-17- (3,5-dinitrobenzoyl)-4-heptadecene (10) that becomes fluorescent upon hydrolysis of its N-acyl bond. This novel substrate was used to study several kinetic aspects of the recombinant CDase from the pathogenic bacterium Pseudomonas aeruginosa PA01. Maximum CDase activity was observed above 1.5 μM substrate, with an apparent Km of 0.5±0.1 μM and a turnover of 5.5 min-1. CDase activity depends on divalent cations without a strong specificity. CDase is inhibited by sphingosine and by several sphingosine analogues. The lack of inhibition by several mammalian CDase inhibitors such as D-erythro-MAPP, L-erythro-MAPP or N-oleoylethanolamine points to a novel active site and/or substrate binding region. The CDase assay described here offers the opportunity to develop and screen for specific bacterial CDase inhibitors of pharmaceutical interest.
Synthesis and intermembrane transfer of pyrene-labelled liponucleotides: Ceramide phosphothymidines
Oskolkova, Olga V.,Shvets, Vitaly I.,Hermetter, Albin,Paltauf, Fritz
, p. 73 - 86 (2007/10/03)
Phospholipid conjugates of 3'-azido-3'-deoxythymidine (AZT) show activity against human immunodeficiency virus (HIV) in vitro. Here we report on the synthesis and characterization of two pyrene containing conjugates: 2-N-(4-(pyren-1-yl)butanoyl)ceramide 5'-phosphothymidine (Pbs-Cer-P-T) (XII) and 2-N-(10-(pyren-1-yl)decanoyl)ceramide 5'-phosphothymidine (Pds-Cer-P-T) (XIII). These fluorescent labelled conjugates served as model compounds to study incorporation of sphingoliponucleotides into membranes. The complex compounds were prepared by condensation of 3'-acetylthymidine and labelled ceramides using the phosphite triester coupling procedure. UV absorption, fluorimetry as well as 1H-, 31P-, 13C-NMR analyses were used for structure confirmation of the synthesized substances. When incorporated into small unilamellar 1-palmitoyl-2-oleoyl-glycerophosphatidylcholine (POPC) vesicles and incubated with unlabelled acceptor POPC vesicles, the compounds (XII) and (XIII) exhibited spontaneous transfer. Kinetic data suggest that transfer from donor to acceptor vesicles occurred via the intervening aqueous phase. The non-specific lipid transfer protein from bovine liver stimulated the transfer of Pds-Cer-P-T between phospholipid vesicles in a concentration dependent manner. Copyright (C) 1999 Elsevier Science Ireland Ltd.
Liposomal Membranes. 2. Synthesis of a Novel Pyrene-Labeled Lecithin and Structural Studies on Liposomal Bilayers
Sunamoto, Junzo,Kondo, Hiroki,Nomura, Tadashi,Okamoto, Hiroshi
, p. 1146 - 1152 (2007/10/02)
A novel pyrene-labeled phosphatidylcholine, 1,2-bis-sn-glycero-3-phosphorylcholine (DPDL), was synthesized for use in structural studies on the liposomal bilayers.From the fluorescence measurements on DPDL incorporated into the phospholipid bilayers as well as in organic solvents and aqueous buffered solutions, the following interesting information was obtained. (1) The probe DPDL is intercalated in a well-ordered fashion in the very hydrophobic domain of egg and dipalmitoylphosphatidylcholine bilayers. (2) Without cholesterol and /or below the phase-transition temperature, DPDL is arranged with the lipid-separated conformation in the shrunk liposomal bilayers (Figure 9d). (3) Increasing the mobility of lipid molecules by the addition of cholesterol and/or by elevating temperatures causes a conformational change of DPDL in the bilayers from the lipid-separated conformation to the intimate one (Figure 9c).
