Design and implementation of an ribonucleic acid (RNA) directed fragment library.

The design of RNA binding ligands is complicated by issues of specificity, target flexibility, and the tractability of known RNA inhibitors toward chemical derivitization. To address these difficulties, an RNA-directed fragment compound library is presented. We began with an analysis of 120 small molecules with reported RNA-binding activity.

Monitoring the effect of three humic acids on a model membrane system using 31P NMR.

The sorption of three humic acids to 1,2-dipalmitoyl-sn-glycero-3-phosphocholine multilamellar vesicle model membrane systems was studied by phosphorus nuclear magnetic resonance (31P NMR). The effects of temperature and pH were investigated. The gel --> bilayer transition did not appear to be affected by any of the humic acids at pH 7; however, all three humic acids induced a perturbation to this transition and to the bilayer structure at pH 4.

V-ATPase inhibition prevents recovery from anoxia in Artemia franciscana embryos: quiescence signaling through dissipation of proton gradients.

The metabolic downregulation critical for long-term survival of Artemia franciscana embryos under anoxia is mediated, in part, by a progressive intracellular acidification. However, very little is known about the mechanisms responsible for the pH transitions associated with exposure to, and recovery from, oxygen deprivation. In the present study, we demonstrate with 31P-NMR that incubation of intact embryos with the V-ATPase inhibitor bafilomycin A1 severely limits intracellular alkalinization during recovery from anoxia without affecting the restoration of cellular nucleotide triphosphate levels.

Chromophore formation in resorcinarene solutions and the visual detection of mono- and oligosaccharides.

The colorimetric properties of resorcinarene solutions had not been investigated since Baeyer's initial synthesis. We recently reported that solutions containing resorcinarene macrocycles develop color upon heating or standing. In the presence of saccharides, these solutions exhibit significant color changes which are easily seen.

Infrared spectroscopy of human apolipoprotein fragments in SDS/D2O: relative lipid-binding affinities and a novel amide I assignment.

Infrared absorption spectra are reported for six apolipoprotein fragments in SDS/D2O. Five of the peptides correspond to proposed lipid-binding domains of human apolipoproteins [apoC-I(7-24), apoC-I(35-53), apoA-II(18-30)+, apoA-I(166-185), apoE(267-289)], and the sixth is the de novo lipid associating peptide LAP-20. The amide I infrared absorption patterns are generally consistent with predominantly helical structures (as determined previously by NMR spectroscopy and distance geometry calculations) and further suggest that apoA-I(166-185) and apoE(267-289) are bound to SDS relatively weakly in comparison to the other four peptides.