Calcium Paraaminosalicylate Hydrate

Exptl. exploration of the vast number of potentially effective organic inhibitors presents a major bottleneck in finding suitable alternatives for chromate-based corrosion inhibitors as the quantities of these organic compounds are essentially infinite.To tackle this challenge, a multi-well exptl. method for corrosion inhibitor screening has been proposed in this work.The inhibition effect and pitting factor of 229 potential inhibitors were determined by profilometry anal. using the high-throughput experimentThe accuracy is validated by traditional gravimetric weight loss anal.The obtained results indicate that the developed approach is of great significance in accelerating the discovery and application of dissolution modulators.

Tuberculosis (TB), caused by Mycobacterium tuberculosis (Mtb), represents a global health challenge, necessitating new treatments with distinct mechanisms of action (MOA) to combat drug resistance. Chuangxinmycin (CM), characterized by its indole-dihydrothiopyran heterocyclic skeleton, exhibits potent antibacterial activity both in vitro and in vivo, with a minimum inhibitory concentration (MIC) of 0.25 μg/mL against Mtb. However, the MOA of CM against Mtb has remained obscure. Through comprehensive genetic, chemical rescue, and protein-drug interaction studies, coupled with biochemical analyses, we reveal that CM selectively binds and inhibits tryptophanyl-tRNA synthetase (TrpRS) encoded by trpS, rather than anthranilate synthase (TrpE). Overexpression of trpS in Mtb results in a 128-fold increase in the MIC of CM, indicating a fundamental cause of resistance, whereas overexpression of trpE leads to modest resistance, suggesting a secondary effect. Conversely, knockdown of trpS or trpE enhances the susceptibility of Mtb to CM. Meanwhile, promoters of trpS in CM-resistant Mtb mutants exhibit increased activity compared to the wild type. Furthermore, drug-protein interaction and biochemical assays have confirmed that while CM effectively inhibits TrpRS, mutants of TrpE show decreased affinity for tryptophan. These results establish that CM exerts its anti-Mtb effects by interfering with the tryptophan-tRNA linkage essential for protein synthesis.