Total Synthesis of Tiacumicin A. Total Synthesis, Relay Synthesis, and Degradation Studies of Fidaxomicin (Tiacumicin B, Lipiarmycin A3)

2018 ◽  
Vol 83 (13) ◽  
pp. 7180-7205 ◽  
Author(s):  
Hiromu Hattori ◽  
Elias Kaufmann ◽  
Hideki Miyatake-Ondozabal ◽  
Regina Berg ◽  
Karl Gademann
Keyword(s):  
Total Synthesis ◽  
Degradation Studies ◽  
Synthesis And Degradation

Synthesis and Degradation Studies of Novel Calcium Polyphosphates

2007 ◽  
Vol 361-363 ◽  
pp. 11-14 ◽  
Author(s):  
Lauren E. Jackson ◽  
Liam M. Grover ◽  
Adrian J. Wright
Keyword(s):  
Thermodynamic Stability ◽  
Comparative Investigation ◽  
Degradation Studies ◽  
Synthesis And Degradation

This paper describes a comparative investigation into the in vitro solubility of the calcium polyphosphates, γ-Ca(PO3)2 and β-Ca(PO3)2. The differing arrangement of their polyphosphates chains appears to result in significant dissolution of γ-Ca(PO3)2 polymorph over the β-Ca(PO3)2 polymorph, which exhibits limited dissolution. These properties are discussed with respect to structure and thermodynamic stability.

Dithiothreitol-based polyurethanes. Synthesis and degradation studies

2010 ◽  
Vol 95 (9) ◽  
pp. 1480-1487 ◽  
Author(s):  
Cristina Ferris ◽  
M. Violante de Paz ◽  
Francisca Zamora ◽  
Juan A. Galbis
Keyword(s):  
Degradation Studies ◽  
Synthesis And Degradation

scholarly journals Total synthesis of the isoquinolinium metabolite ETM-204 of Trabectidin

2021 ◽  
Author(s):  
Christian Lembacher-Fadum ◽  
Simon Gissing ◽  
Georg Pour ◽  
Rolf Breinbauer
Keyword(s):  
Ovarian Cancer ◽  
Soft Tissue ◽  
Soft Tissue Sarcoma ◽  
Total Synthesis ◽  
Ph Dependence ◽  
Spectroscopic Characterization ◽  
Pharmaceutical Drug ◽  
Central Elements ◽  
Degradation Studies ◽  
Ecteinascidin 743

AbstractEcteinascidin-743 (Trabectidin, Trabectedin®, Yondelis®) is a synthetically obtained pharmaceutical drug originally isolated from a marine tunicate. Trabectedin is used for the chemotherapy of soft-tissue sarcoma and ovarian cancer. The isoquinolinium metabolite ETM-204 has been found in biotransformation and degradation studies of Trabectedin. We report the first total synthesis of ETM-204 and its full spectroscopic characterization confirming the postulated structure. Central elements of the 12-step synthesis starting from 2-methyl-6-nitrophenol are a Cu-mediated conversion of an iodoarene to a phenol, a Skattebøl-formylation, and a modified Pomeranz–Fritsch cyclization to assemble the isoquinoline ring. The pH-dependence of its visual absorbance could be clarified. Graphic abstract

scholarly journals Synthesis and degradation of phosphoenolpyruvate carboxylase in rat liver and adipose tissue. Changes during a starvation–re-feeding cycle

1973 ◽  
Vol 134 (2) ◽  
pp. 445-453 ◽  
Author(s):  
M. F. Hopgood ◽  
F. J. Ballard ◽  
Lea Reshef ◽  
R. W. Hanson
Keyword(s):  
Adipose Tissue ◽  
Total Synthesis ◽  
Phosphoenolpyruvate Carboxylase ◽  
Degradation Rate ◽  
Relative Rate ◽  
Enzyme Synthesis ◽  
Starvation Period ◽  
Feeding Cycle ◽  
Tissue Changes ◽  
Synthesis And Degradation

A specific antibody against liver cytosol phosphoenolpyruvate carboxylase (EC 4.1.1.32) was used to isolate the enzyme from liver and adipose tissue. With this technique we have shown that phosphoenolpyruvate carboxylase synthesis in starved rats accounts for 3% of the total synthesis of cytosol protein in each tissue. Re-feeding starved animals decreases this relative rate of phosphoenolpyruvate carboxylase synthesis to 0.2% and 1% respectively in liver and adipose tissue, and the activity of the enzyme in each tissue is decreased to 25% of the starvation value. An additional starvation period is accompanied by an increased rate of enzyme synthesis, but the response to starvation is considerably slower than that caused by re-feeding. The degradation rate of phosphoenolpyruvate carboxylase is also subject to regulation. Thus re-feeding starved animals decreases the half-life of the enzyme in liver from 13h to 5.2h, but the rapid rate of degradation is maintained at least during the first 20h of subsequent starvation. Only slight changes in the degradation rate of phosphoenolpyruvate carboxylase are found in adipose tissue. We conclude that the large alterations in the rate of enzyme synthesis during a starvation–re-feeding cycle are the major cause of fluctuations in activity.

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