Influence of the biological fluid on the corrosion of dental amalgam

An electrochemical study of corrosion of Tytin® dental amalgam was carried out in electrolytes similar to body fluids: artificial saliva with or without lactic acid, a polymer-containing product of the same composition as Glandosane® and in Krebs-Ringer solution. The electrochemical techniques of open circuit potential, polarisation curves, cyclic voltammetry and electrochemical impedance were employed as a function of immersion time to characterise the surface processes occurring and bring out the differences between the different solutions. The influence of pH was tested in solutions of artificial saliva with or without lactic acid. The results demonstrated the importance of the organic component on the rate of corrosion and of adsorption phenomena on the amalgam surface.http://www.sciencedirect.com/science/article/B6TWS-4CBW449-2/1/0a518cbfe9cf78ca47335cef9310f2b

Natural product coumarins that inhibit human carbonic anhydrases.

Natural products (NPs) have proven to be an invaluable source of new chemotherapies yet very few have been explored to source small molecule carbonic anhydrase (CA) inhibitors. CA enzymes underpin physiological pH and are critical to the progression of several diseases including cancer. The present study is the first to more widely investigate NP coumarins for CA inhibition following the recent discovery of a NP coumarin CA inhibitor. We assembled a NP library comprising 24 plant coumarins (compounds 4-27) and three ascidian coumarins (compounds 28-30) that together provide a diverse collection of structures containing the coumarin pharmacophore. This library was then evaluated for inhibition of six human CA isozymes (CAs I, II, VII, IX, XII and XIII) and a broad range of inhibition and isozyme selectivity profiles were evident. Our findings provide a platform to support further evaluation of NPs for the discovery of new chemotypes that inhibit disease relevant CA enzymes.Full Tex

Natural product polyamines that inhibit human carbonic anhydrases

Natural product compound collections have proven an effective way to access chemical diversity and recent findings have identified phenolic, coumarin, and polyamine natural products as atypical chemotypes that inhibit carbonic anhydrases (CAs). CA enzymes are implicated as targets of variable drug therapeutic classes and the discovery of selective, drug-like CA inhibitors is essential. Just two natural product polyamines, spermine and spermidine, have until now been investigated as CA inhibitors. In this study, five more complex natural product polyamines 1–5, derived from either marine sponge or fungi, were considered for inhibition of six different human CA isozymes of interest in therapeutic drug development. All compounds share a simple polyamine core fragment, either spermine or spermidine, yet display substantially different structure activity relationships for CA inhibition. Notably, polyamines 1–5 were submicromolar inhibitors of the cancer drug target CA IX, this is more potent than either spermine or spermidine

Glycosyl Coumarin Carbonic Anhydrase IX and XII Inhibitors Strongly Attenuate the Growth of Primary Breast Tumors.

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