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180851-50-7

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180851-50-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 180851-50-7 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,8,0,8,5 and 1 respectively; the second part has 2 digits, 5 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 180851-50:
(8*1)+(7*8)+(6*0)+(5*8)+(4*5)+(3*1)+(2*5)+(1*0)=137
137 % 10 = 7
So 180851-50-7 is a valid CAS Registry Number.

180851-50-7Relevant articles and documents

Structure of a complex formed by a protein and a helical aromatic oligoamide foldamer at 2.1 ? resolution

Buratto, Jérémie,Colombo, Cinzia,Stupfel, Marine,Dawson, Simon J.,Dolain, Christel,Langlois D'Estaintot, Béatrice,Fischer, Lucile,Granier, Thierry,Laguerre, Michel,Gallois, Bernard,Huc, Ivan

, p. 883 - 887 (2014)

In the search of molecules that could recognize sizeable areas of protein surfaces, a series of ten helical aromatic oligoamide foldamers was synthesized on solid phase. The foldamers comprise three to five monomers carrying various proteinogenic side chains, and exist as racemic mixtures of interconverting right-handed and left-handed helices. Functionalization of the foldamers by a nanomolar ligand of human carbonic anhydrase II (HCA) ensured that they would be held in close proximity to the protein surface. Foldamer-protein interactions were screened by circular dichroism (CD). One foldamer displayed intense CD bands indicating that a preferred helix handedness is induced upon interacting with the protein surface. The crystal structure of the complex between this foldamer and HCA could be resolved at 2.1 ? resolution and revealed a number of unanticipated protein-foldamer, foldamer-foldamer, and protein-protein interactions. To design a foldamer that binds to a protein surface, a strategy is proposed that uses a known protein ligand to tether the foldamer to the protein surface. Candidates are first screened for induced circular dichroism in presence of the protein. Then, structural information about foldamer-protein interactions is collected before strong binding is established. The crystal structure of human carbonic anhydrase (A, B chains) with helical aromatic amide foldamers (stick models) is shown. Copyright

177. Electrospray-ionization mass spectrometry part 2: Neighboring-group participation in the mass-spectral decomposition of 4-hydroxycinnamoyl-spermidines

Hu, Wenqing,Reder, Elke,Hesse, Manfred

, p. 2137 - 2151 (1996)

The three mono substituted N-[(E)-3-(4-hydroxyphenyl)prop-2-enoyl]spermidines 1-3 have been studied by positive-ion electrospray-ionization tandem mass spectrometry (ESI-MS/MS). Because of the neighboring-group participation, the MS/MS of [1 + H]+/s

COMPOUNDS AND USES THEREOF

-

, (2021/08/06)

The present disclosure features compounds and methods useful for the treatment of BAF complex-related disorders.

Azido-Desferrioxamine Siderophores as Functional Click-Chemistry Probes Generated in Culture upon Adding a Diazo-Transfer Reagent

Gotsbacher, Michael P.,Codd, Rachel

, p. 1433 - 1445 (2020/02/27)

This work aimed to undertake the in situ conversion of the terminal amine groups of bacterial desferrioxamine (DFO) siderophores, including desferrioxamine B (DFOB), to azide groups to enable downstream click chemistry. Initial studies trialed a precursor-directed biosynthesis (PDB) approach. Supplementing Streptomyces pilosus culture with blunt-end azido/amine non-native substrates designed to replace 1,5-diaminopentane as the native diamine substrate in the terminal amine position of DFOB did not produce azido-DFOB. Addition of the diazo-transfer reagent imidazole-1-sulfonyl azide hydrogen sulfate to spent S. pilosus medium that had been cultured in the presence of 1,4-diaminobutane, as a viable native substrate to expand the suite of native DFO-type siderophores, successfully generated the cognate suite of azido-DFO analogues. CuI-mediated or strain-promoted CuI-free click chemistry reactions between this minimally processed mixture and the appropriate alkyne-bearing biotin reagents produced the cognate suite of 1,4-disubstituted triazole-linked DFO-biotin compounds as potential molecular probes, detected as FeIII-loaded species. The amine-to-azide transformation of amine-bearing natural products in complex mixtures by the direct addition of a diazo-transfer reagent to deliver functional click chemistry reagents adds to the toolbox for chemical proteomics, chemical biology, and drug discovery.

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