[NMR paper] Liver-Targeted Small Molecule Inhibitors of Proprotein Convertase Subtilisin/Kexin Type 9 Synthesis
Liver-Targeted Small Molecule Inhibitors of Proprotein Convertase Subtilisin/Kexin Type 9 Synthesis
Targeting of the human ribosome is an unprecedented therapeutic modality with a genome-wide selectivity challenge. Herein we describe a liver-targeted drug candidate that inhibits ribosomal synthesis of PCSK9, a lipid regulator considered undruggable by small molecules. Key to the concept was the identification of pharmacologically active zwitterions designed to be retained in the liver. Oral delivery of the poorly permeable zwitterions was achieved via prodrugs susceptible to cleavage by...
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10-27-2017 02:54 AM
[NMR paper] Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR
Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR
Carbohydrate-based vaccines are among the safest and most effective vaccines and represent potent tools for prevention of life-threatening bacterial infectious diseases, like meningitis and pneumonia. The chemical conjugation of a weak antigen to protein as a source of T-cell epitopes generates a glycoconjugate vaccine, that results more immunogenic. Several methods have been used so far to characterize the resulting polysaccharide-protein conjugates. However, a reduced number of methodologies has...
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10-10-2017 09:37 PM
[NMR paper] Orthogonal spin labeling using click chemistry for in vitro and in vivo applications
Orthogonal spin labeling using click chemistry for in vitro and in vivo applications
Publication date: Available online 2 December 2016
Source:Journal of Magnetic Resonance</br>
Author(s): Svetlana Kucher, Sergei Korneev, Swati Tyagi, Ronja Apfelbaum, Dina Grohmann, Edward A. Lemke, Johann P. Klare, Heinz-Jürgen Steinhoff, Daniel Klose</br>
Site-directed spin labeling for EPR- and NMR spectroscopy has mainly been achieved exploiting the specific reactivity of cysteines. For proteins with native cysteines or for in vivo applications, an alternative...
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12-03-2016 02:09 PM
[NMR paper] Protein-Observed Fluorine NMR: A Bioorthogonal Approach for Small Molecule Discovery.
Protein-Observed Fluorine NMR: A Bioorthogonal Approach for Small Molecule Discovery.
Protein-Observed Fluorine NMR: A Bioorthogonal Approach for Small Molecule Discovery.
J Med Chem. 2015 Nov 24;
Authors: Arntson KE, Pomerantz WC
Abstract
The 19F isotope is 100% naturally abundant and is the second most sensitive and stable NMR-active nucleus. Unlike the ubiquitous hydrogen atom, fluorine is nearly absent in biological systems, making it a unique bioorthogonal atom for probing molecular interactions in biology. Over 73...
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11-26-2015 12:13 AM
Diels-Alder reactionâ??triggered bioorthogonal protein decaging in living cells - Nature.com
Diels-Alder reactionâ??triggered bioorthogonal protein decaging in living cells - Nature.com
<img alt="" height="1" width="1" />
Diels-Alder reactionâ??triggered bioorthogonal protein decaging in living cells
Nature.com
A generally applicable strategy, however, remains elusive. Herein we describe a small moleculeâ??triggered bioorthogonal protein decaging technique that relies on the inverse electron-demand Diels-Alder reaction for eliminating a chemically caged protein ...
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11-04-2014 02:32 PM
¿¿PT: a comprehensive toolbox for the analysis of protein motion - 7thSpace Interactive (press release)
¿¿PT: a comprehensive toolbox for the analysis of protein motion - 7thSpace Interactive (press release)
<img alt="" height="1" width="1" />
¿¿PT: a comprehensive toolbox for the analysis of protein motion
7thSpace Interactive (press release)
Normal Mode Analysis is one of the most successful techniques for studying motions in proteins and macromolecules. It can provide information on the mechanism of protein functions, used to aid crystallography and NMR data reconstruction, and calculate ...
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06-07-2013 10:42 PM
[NMR paper] Characterization of covalent protein conjugates using solid-state 13C NMR spectroscop
Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Related Articles Characterization of covalent protein conjugates using solid-state 13C NMR spectroscopy.
Biochemistry. 1991 Jul 23;30(29):7057-62
Authors: Garbow JR, Fujiwara H, Sharp CR, Logusch EW
Cross-polarization magic-angle spinning (CPMAS) 13C NMR spectroscopy has been used to characterize covalent conjugates of alachlor, an alpha-chloroacetamide hapten, with glutathione (GSH) and bovine serum albumin (BSA). The solid-state NMR method demonstrates...