scholarly journals Experimentally Quantifying Small-Molecule Bond Activation Using Valence-to-Core X-ray Emission Spectroscopy

2013 ◽  
Vol 135 (32) ◽  
pp. 11803-11808 ◽  
Author(s):  
Christopher J. Pollock ◽  
Katarzyna Grubel ◽  
Patrick L. Holland ◽  
Serena DeBeer
Keyword(s):  
Small Molecule ◽  
Emission Spectroscopy ◽  
Bond Activation ◽  
X Ray

scholarly journals Valence‐to‐Core X‐ray Emission Spectroscopy as a Probe of O−O Bond Activation in Cu 2 O 2 Complexes

2019 ◽  
Vol 58 (27) ◽  
pp. 9114-9119 ◽  
Author(s):  
George E. Cutsail ◽  
Nicole L. Gagnon ◽  
Andrew D. Spaeth ◽  
William B. Tolman ◽  
Serena DeBeer
Keyword(s):  
Emission Spectroscopy ◽  
Bond Activation ◽  
X Ray

Valence‐to‐Core X‐ray Emission Spectroscopy as a Probe of O−O Bond Activation in Cu 2 O 2 Complexes

2019 ◽  
Vol 131 (27) ◽  
pp. 9212-9217 ◽  
Author(s):  
George E. Cutsail ◽  
Nicole L. Gagnon ◽  
Andrew D. Spaeth ◽  
William B. Tolman ◽  
Serena DeBeer
Keyword(s):  
Emission Spectroscopy ◽  
Bond Activation ◽  
X Ray

Signal/Noise Ratio and Elemental Detectivity by Eels

1982 ◽  
Vol 40 ◽  
pp. 488-489
Author(s):  
R. F. Egerton
Keyword(s):  
Energy Loss ◽  
Electron Energy ◽  
Elemental Analysis ◽  
Electron Energy Loss Spectroscopy ◽  
Emission Spectroscopy ◽  
X Ray ◽  
Signal Noise ◽  
Characteristic Signal ◽  
Noise Ratio ◽  
Electron Energy Loss

An important parameter governing the sensitivity and accuracy of elemental analysis by electron energy-loss spectroscopy (EELS) or by X-ray emission spectroscopy is the signal/noise ratio of the characteristic signal.

Recent Development of Small Molecule Glutaminase Inhibitors

2018 ◽  
Vol 18 (6) ◽  
pp. 432-443 ◽  
Author(s):  
Minsoo Song ◽  
Soong-Hyun Kim ◽  
Chun Young Im ◽  
Hee-Jong Hwang
Keyword(s):  
Small Molecule ◽  
Cell Metabolism ◽  
Phase 1 ◽  
Vital Role ◽  
Glutamine Metabolism ◽  
Inhibition Mechanism ◽  
Tumor Cell Growth ◽  
X Ray ◽  
New Class ◽  
Preclinical And Clinical Studies

Glutaminase (GLS), which is responsible for the conversion of glutamine to glutamate, plays a vital role in up-regulating cell metabolism for tumor cell growth and is considered to be a valuable therapeutic target for cancer treatment. Based on this important function of glutaminase in cancer, several GLS inhibitors have been developed in both academia and industry. Most importantly, Calithera Biosciences Inc. is actively developing the glutaminase inhibitor CB-839 for the treatment of various cancers, and it is currently being evaluated in phase 1 and 2 clinical trials. In this review, recent efforts to develop small molecule glutaminase inhibitors that target glutamine metabolism in both preclinical and clinical studies are discussed. In particular, more emphasis is placed on CB-839 because it is the only small molecule GLS inhibitor being studied in a clinical setting. The inhibition mechanism is also discussed based on X-ray structure studies of thiadiazole derivatives present in glutaminase inhibitor BPTES. Finally, recent medicinal chemistry efforts to develop a new class of GLS inhibitors are described in the hopes of providing useful information for the next generation of GLS inhibitors.

scholarly journals Phosphorus Kβ X-Ray emission spectroscopy detects non-covalent interactions of phosphate biomolecules in situ

2021 ◽  
Author(s):  
Zachary Mathe ◽  
Olivia McCubbin Stepanic ◽  
Sergey Peredkov ◽  
Serena DeBeer
Keyword(s):  
Nucleic Acids ◽  
Emission Spectroscopy ◽  
Adenine Nucleotides ◽  
X Ray ◽  
Non Covalent Interactions ◽  
Covalent Interactions ◽  
Phosphate Groups

Phosphorus is ubiquitous in biochemistry, found in the phosphate groups of nucleic acids and the energy-transferring system of adenine nucleotides (e.g. ATP). Kβ X-ray emission spectroscopy (XES) at phosphorus has...

scholarly journals Backbonding contributions to small molecule chemisorption in a metal–organic framework with open copper(i) centers

2021 ◽  
Author(s):  
Gregory M. Su ◽  
Han Wang ◽  
Brandon R. Barnett ◽  
Jeffrey R. Long ◽  
David Prendergast ◽  
...  
Keyword(s):  
Fine Structure ◽  
Small Molecule ◽  
Metal Organic Framework ◽  
X Ray ◽  
Metal Site ◽  
Absorption Fine ◽  
Metal Organic ◽  
X Ray Absorption ◽  
Organic Framework

In situ near edge X-ray absorption fine structure spectroscopy directly probes unoccupied states associated with backbonding interactions between the open metal site in a metal–organic framework and various small molecule guests.

scholarly journals A small molecule compound with an indole moiety inhibits the main protease of SARS-CoV-2 and blocks virus replication

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Shin-ichiro Hattori ◽  
Nobuyo Higashi-Kuwata ◽  
Hironori Hayashi ◽  
Srinivasa Rao Allu ◽  
Jakka Raghavaiah ◽  
...  
Keyword(s):  
Small Molecule ◽  
Covalent Bond ◽  
Amino Acid Residues ◽  
X Ray ◽  
Viral Breakthrough ◽  
Main Protease ◽  
Small Molecule Compound ◽  
Polar Interactions ◽  
High Concentrations

AbstractExcept remdesivir, no specific antivirals for SARS-CoV-2 infection are currently available. Here, we characterize two small-molecule-compounds, named GRL-1720 and 5h, containing an indoline and indole moiety, respectively, which target the SARS-CoV-2 main protease (Mpro). We use VeroE6 cell-based assays with RNA-qPCR, cytopathic assays, and immunocytochemistry and show both compounds to block the infectivity of SARS-CoV-2 with EC50 values of 15 ± 4 and 4.2 ± 0.7 μM for GRL-1720 and 5h, respectively. Remdesivir permitted viral breakthrough at high concentrations; however, compound 5h completely blocks SARS-CoV-2 infection in vitro without viral breakthrough or detectable cytotoxicity. Combination of 5h and remdesivir exhibits synergism against SARS-CoV-2. Additional X-ray structural analysis show that 5h forms a covalent bond with Mpro and makes polar interactions with multiple active site amino acid residues. The present data suggest that 5h might serve as a lead Mpro inhibitor for the development of therapeutics for SARS-CoV-2 infection.

scholarly journals Probing physical oxidation state via resonant X‐ray emission spectroscopy: Applications to iron model complexes and nitrogenase

2021 ◽  
Author(s):  
Serena DeBeer ◽  
Rebeca G. Castillo ◽  
Anselm W. Hahn ◽  
Benjamin E. Van Kuiken ◽  
Justin T. Henthorn
Keyword(s):  
Oxidation State ◽  
Emission Spectroscopy ◽  
Model Complexes ◽  
X Ray

scholarly journals Arsenoplatin-Ferritin Nanocage: Structure and Cytotoxicity

2021 ◽  
Vol 22 (4) ◽  
pp. 1874
Author(s):  
Giarita Ferraro ◽  
Alessandro Pratesi ◽  
Damiano Cirri ◽  
Paola Imbimbo ◽  
Daria Maria Monti ◽  
...  
Keyword(s):  
Biological Activity ◽  
Diffraction Data ◽  
Inductively Coupled Plasma ◽  
Emission Spectroscopy ◽  
Atomic Emission ◽  
Side Chain ◽  
Plasma Atomic Emission ◽  
Average Amount ◽  
X Ray ◽  
Inductively Coupled

Arsenoplatin-1 (AP-1), the prototype of a novel class of metallodrugs containing a PtAs(OH)2 core, was encapsulated within the apoferritin (AFt) nanocage. UV-Vis absorption spectroscopy and inductively coupled plasma-atomic emission spectroscopy measurements confirmed metallodrug encapsulation and allowed us to determine the average amount of AP-1 trapped inside the cage. The X-ray structure of AP-1-encapsulated AFt was solved at 1.50 Å. Diffraction data revealed that an AP-1 fragment coordinates the side chain of a His residue. The biological activity of AP-1-loaded AFt was comparatively tested on a few representative cancer and non-cancer cell lines. Even though the presence of the cage reduces the overall cytotoxicity of AP-1, it improves its selectivity towards cancer cells.

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