The mechanism of neutral amino acid decomposition in the gas phase. The elimination kinetics ofN,N-dimethylglycine ethyl ester, ethyl 1-piperidineacetate, andN,N-dimethylglycine

2001 ◽  
Vol 33 (8) ◽  
pp. 465-471 ◽  
Author(s):  
Adolfo Ensuncho ◽  
M. Jennifer Lafont ◽  
Alexandra Rotinov ◽  
Rosa M. Domínguez ◽  
Armando Herize ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gas Phase ◽  
Ethyl Ester ◽  
Neutral Amino Acid ◽  
Acid Decomposition ◽  
Elimination Kinetics

The kinetics and mechanisms of gas phase elimination of the ethyl ester of amino acid hydrochlorides

2006 ◽  
Vol 19 (5) ◽  
pp. 326-332 ◽  
Author(s):  
Gabriel Chuchani ◽  
Armando Herize ◽  
Rosa María Domínguez ◽  
Alexandra Rotinov ◽  
Maria Tosta
Keyword(s):  
Amino Acid ◽  
Gas Phase ◽  
Ethyl Ester ◽  
Phase Elimination

Theoretical study of the gas-phase decomposition of neutral α-amino acid ethyl esters. Part 1-The elimination ofN,N-dimethylglycine ethyl ester and ethyl 1-piperidineacetate

2002 ◽  
Vol 15 (7) ◽  
pp. 413-419 ◽  
Author(s):  
Jairo Quijano ◽  
Rafael Notario ◽  
Eduardo Chamorro ◽  
Luis A. León ◽  
Claudia Sánchez ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gas Phase ◽  
Ethyl Ester ◽  
Theoretical Study ◽  
Ethyl Esters ◽  
Phase Decomposition

scholarly journals Identification and Characterization of Inhibitors of a Neutral Amino Acid Transporter, SLC6A19, Using Two Functional Cell-Based Assays

2018 ◽  
Vol 24 (2) ◽  
pp. 111-120 ◽  
Author(s):  
Sanjay J. Danthi ◽  
Beirong Liang ◽  
Oanh Smicker ◽  
Benjamin Coupland ◽  
Jill Gregory ◽  
...  
Keyword(s):  
Amino Acid ◽  
High Throughput Screening ◽  
Amino Acid Transporter ◽  
Neutral Amino Acid ◽  
Imaging Plate ◽  
Acid Uptake ◽  
Functional Assays ◽  
Neutral Amino Acid Transporter ◽  
Acid Transporter ◽  
Pharmacologically Active

SLC6A19 (B0AT1) is a neutral amino acid transporter, the loss of function of which results in Hartnup disease. SLC6A19 is also believed to have an important role in amino acid homeostasis, diabetes, and weight control. A small-molecule inhibitor of human SLC6A19 (hSLC6A19) was identified using two functional cell-based assays: a fluorescence imaging plate reader (FLIPR) membrane potential (FMP) assay and a stable isotope-labeled neutral amino acid uptake assay. A diverse collection of 3440 pharmacologically active compounds from the Microsource Spectrum and Tocriscreen collections were tested at 10 µM in both assays using MDCK cells stably expressing hSLC6A19 and its obligatory subunit, TMEM27. Compounds that inhibited SLC6A19 activity in both assays were further confirmed for activity and selectivity and characterized for potency in functional assays against hSLC6A19 and related transporters. A single compound, cinromide, was found to robustly, selectively, and reproducibly inhibit SLC6A19 in all functional assays. Structurally related analogs of cinromide were tested to demonstrate structure–activity relationship (SAR). The assays described here are suitable for carrying out high-throughput screening campaigns to identify modulators of SLC6A19.

scholarly journals B0AT1 amino acid transporter complexed with SARS-CoV-2 receptor ACE2 forms a heterodimer functional unit: in situ conformation using radiation inactivation analysis

Function ◽  
2021 ◽  
Author(s):  
Bruce R Stevens ◽  
J Clive Ellory ◽  
Robert L Preston
Keyword(s):  
Amino Acid ◽  
Membrane Trafficking ◽  
Functional Unit ◽  
Membrane Vesicles ◽  
High Energy ◽  
Amino Acid Transporter ◽  
Neutral Amino Acid ◽  
Transport Activity ◽  
Acid Transporter

Abstract The SARS-CoV-2 receptor, Angiotensin Converting Enzyme-2 (ACE2), is expressed at levels of greatest magnitude in the small intestine as compared to all other human tissues. Enterocyte ACE2 is co-expressed as the apical membrane trafficking partner obligatory for expression and activity of the B0AT1 sodium-dependent neutral amino acid transporter. These components are assembled as an [ACE2: B0AT1]2 dimer-of-heterodimers quaternary complex that putatively steers SARS-CoV-2 tropism in the gastrointestinal (GI) tract. GI clinical symptomology is reported in about half of COVID-19 patients, and can be accompanied by gut shedding of virion particles. We hypothesized that within this 4-mer structural complex, each [ACE2: B0AT1] heterodimer pair constitutes a physiological “functional unit.” This was confirmed experimentally by employing purified lyophilized enterocyte brush border membrane vesicles that were exposed to increasing doses of high-energy electron radiation from a 16 MeV linear accelerator. Based on established target theory, the results indicated the presence of Na+-dependent neutral amino acid influx transport activity functional unit with target size mw = 183.7 ± 16.8 kDa in situ in intact apical membranes. Each thermodynamically stabilized [ACE2: B0AT1] heterodimer functional unit manifests the transport activity within the whole ∼345 kDa [ACE2: B0AT1]2 dimer-of-heterodimers quaternary structural complex. The results are consistent with our prior molecular docking modeling and gut-lung axis approaches to understanding COVID-19. These findings advance the understanding of the physiology of B0AT1 interaction with ACE2 in the gut, and thereby potentially contribute to translational developments designed to treat or mitigate COVID-19 variant outbreaks and/or GI symptom persistence in long-haul Post-Acute Sequelae of SARS-CoV-2 (PASC).

scholarly journals UV-A light-assisted gas-phase formic acid decomposition on photo-thermo Ru/TiO2 catalyst

2021 ◽  
Author(s):  
Javier Ivanez ◽  
Patricia Garcia-Munoz ◽  
Agnieszka M. Ruppert ◽  
Nicolas Keller
Keyword(s):  
Formic Acid ◽  
Gas Phase ◽  
Acid Decomposition ◽  
Tio2 Catalyst ◽  
Formic Acid Decomposition
Sign in / Sign up

Export Citation Format

Share Document