Total synthesis of a cyclic adenosine 5'-diphosphate ribose receptor agonist

Stable cyclic adenosine 5'-diphosphate ribose (cADPR) analogues are chemical biology tools that can probe the Ca(2+) release mechanism and structure-activity relationships of this emerging potent second messenger. However, analogues with an intact "northern" ribose have been inaccessible due to the difficulty of generating the sensitive N1-ribosyl link. We report the first total synthesis of the membrane permeant, hydrolytically stable, cADPR receptor agonist 8-Br-N1-cIDPR via regio- and stereoselective N1-ribosylation of protected 8-bromoinosine.     

Coupled absorption filters for thermal detectors

A resonant absorption cavity that couples long-wavelength infrared (LWIR) light into a movable plate has been demonstrated for thermal detectors, especially microbolometers. Each device is continuously tunable over 8.7-11.1 microm by using electrostatic actuation with voltages from 0 to 42 V. The width of the resonance is relatively broad, approximately 1.5 microm, to match the large widths of many spectral features in the LWIR. At an actuation voltage of 45 V, the device switches into a broadband mode with an absorption width of 2.83 microm. This latter mode is used to enhance sensitivity in low-light situations in which little spectral information is present.     

Regioselective hydrolysis of myo-inositol 1,3,5-orthobenzoate via a 1,2-bridged 2'-phenyl-1',3'-dioxolan-2'-ylium ion provides a rapid route to the anticancer agent Ins(1,3,4,5,6)P5

Acid hydrolysis of myo-inositol 1,3,5-orthobenzoate leads regioselectively to 2-O-benzoyl-myo-inositol via a 1,2-bridged 2'-phenyl-1',3'-dioxolan-2'-ylium ion observed by 1H and 13C NMR spectroscopy, providing the precursor for a highly efficient route to the anticancer agent myo-inositol 1,3,4,5,6-pentakisphosphate.     

A comparative study of the single crystal X-ray determination and molecular modelling of the binding of oligomycin to ATP Synthase

Recently published X-ray structures of three common forms, A, B and C, of oligomycin, including absolute configurations, are investigated to examine their binding to ATP Synthase. The X-ray studies reveal regions with differences in three-dimensional structure and hydrogen bonding propensity between the oligomycins, which may be associated with their potential to bind to sites on ATP Synthase. Computational docking studies carried out using MOE with the X-ray structures and an homology model of the F_O domain of ATP Synthase from Escherichia coli, are used to derive an induced fit pocket. Docking of all oligomycins to this pocket indicate that the B and C forms bind more tightly than the A form. Consideration of the single crystal X-ray data alone indicate the B form may be the best inhibitor and that O(24) is the most important ligating group for binding, this is supported by the docking data. The latter reveals Asn214 and other key proton translocating residues to be the main residues contacted by the inhibitor. These data allow the binding modes of different forms of oligomycin to be deduced from X-ray single crystal data supported by molecular modelling and computational docking studies.     

ChemInform Abstract: Lewis Acidities and Hydride,Fluoride, and X‐ Affinities of the BH3‐nXn Compounds for (X: F,Cl, Br,I, NH2, OH,and SH) from Coupled Cluster Theory.

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