12 research outputs found
Synthesis and structure of azole-fused indeno[2,1-c]quinolines and their anti-mycobacterial properties â
Prompted by our discovery of a new class of conformationally-locked indeno[2,1-c]quinolines as anti-mycobacterials, compounds 2a and 3a
Selenoprotein: Potential Player in Redox Regulation in <i>Chlamydomonas reinhardtii</i>
Selenium (Se) is an essential micro-element for many organisms, including Chlamydomonas reinhardtii, and is required in trace amounts. It is obtained from the 21st amino acid selenocysteine (Sec, U), genetically encoded by the UGA codon. Proteins containing Sec are known as selenoproteins. In eukaryotes, selenoproteins are present in animals and algae, whereas fungi and higher plants lack them. The human genome contains 25 selenoproteins, most of which are involved in antioxidant defense activity, redox regulation, and redox signaling. In algae, 42 selenoprotein families were identified using various bioinformatics approaches, out of which C. reinhardtii is known to have 10 selenoprotein genes. However, the role of selenoproteins in Chlamydomonas is yet to be reported. Chlamydomonas selenoproteins contain conserved domains such as CVNVGC and GCUG, in the case of thioredoxin reductase, and CXXU in other selenoproteins. Interestingly, Sec amino acid residue is present in a catalytically active domain in Chlamydomonas selenoproteins, similar to human selenoproteins. Based on catalytical active sites and conserved domains present in Chlamydomonas selenoproteins, we suggest that Chlamydomonas selenoproteins could have a role in redox regulation and defense by acting as antioxidants in various physiological conditions
NMR Method for Simultaneous HostâGuest Binding Constant Measurement
An NMR-based relative
binding affinity measurement method has been
developed in which differences in the binding affinities of different
hosts toward a particular guest (Îlog<i>K</i><sub>ass</sub> values) are measured in the same solution. As an advancement,
the method allows the simultaneous determination of several Îlog<i>K</i><sub>ass</sub> values in a single run. As a proof of principle,
the method was used to measure binding affinity differences of a number
of indolocarbazole- and urea-based synthetic receptors toward acetate
ion in DMSO-<i>d</i><sub>6</sub>/H<sub>2</sub>O (99.5%:0.5%
m/m). As a result, a binding affinity scale containing 33 receptors
and spanning 2.32 log units with excellent self-consistency (consistency
standard deviation = 0.01 log unit) was created. Together with the
very good agreement of the results with those obtained by UVâvis
spectrophotometry, this demonstrates the high accuracy of the method
and the fact that the NMR and UVâvis techniques can be used
interchangeably (in spite of the very different concentrations used
in these techniques). Additionally, it was found for symmetrical receptor
molecules from the same compound family that there is a correlation
between the acetate binding affinity of a receptor and the <sup>15</sup>N chemical shift of the nitrogen atoms of its binding centers
Accurate Method To Quantify Binding in Supramolecular Chemistry
An approach for accurate and comparable measurement of hostâguest binding affinities is introduced whereby differences in binding strength (?logKass values) are measured between two host molecules toward a particular guest under identical solvent conditions. Measuring differences instead of absolute values enables obtaining highly accurate results, because many of the uncertainty sources (the solvation/association state of the guest in solution, deviations in solvent composition, etc.) cancel out. As a proof of concept, this method was applied to the measurement of the binding strength of 28 synthetic anion receptors toward acetate in acetonitrile containing 0.5% water. The receptors included differently substituted indolocarbazoles, ureas, thioureas, and some others. Possible deprotonation of more acidic receptors of each compound class by acetate was checked by measuring their acidities (?pKa values) relative to acetic acid in the same solvent. A self-consistent (consistency standard deviation 0.04 log units) binding affinity scale ranging for around 2.7 log units was constructed from the results. Absolute logKass values were found by anchoring the scale to the absolute logKass values of two receptor molecules, determined independently by direct measurements. This new approach is expected to find use in accurate quantification of a wide range of binding processes relevant to supramolecular chemistry
Accurate Method To Quantify Binding in Supramolecular Chemistry
An
approach for accurate and comparable measurement of hostâguest
binding affinities is introduced whereby differences in binding strength
(Îlog<i>K</i><sub>ass</sub> values) are measured between
two host molecules toward a particular guest under identical solvent
conditions. Measuring differences instead of absolute values enables
obtaining highly accurate results, because many of the uncertainty
sources (the solvation/association state of the guest in solution,
deviations in solvent composition, etc.) cancel out. As a proof of
concept, this method was applied to the measurement of the binding
strength of 28 synthetic anion receptors toward acetate in acetonitrile
containing 0.5% water. The receptors included differently substituted
indolocarbazoles, ureas, thioureas, and some others. Possible deprotonation
of more acidic receptors of each compound class by acetate was checked
by measuring their acidities (Îp<i>K</i><sub>a</sub> values) relative to acetic acid in the same solvent. A self-consistent
(consistency standard deviation 0.04 log units) binding affinity scale
ranging for around 2.7 log units was constructed from the results.
Absolute log<i>K</i><sub>ass</sub> values were found by
anchoring the scale to the absolute log<i>K</i><sub>ass</sub> values of two receptor molecules, determined independently by direct
measurements. This new approach is expected to find use in accurate
quantification of a wide range of binding processes relevant to supramolecular
chemistry