Background: High concentration protein formulation (HCPF) development needs to balance protein stability attributes such as conformational/colloidal stability, chemical stability, and solution properties such as viscosity and osmolality.
Methodology: A three-phase design is established in this work. In Phase 1, conformational and colloidal stability are measured by 384-well-based high-throughput (HT) biophysical screening while viscosity reduction screening is performed with HT viscosity screening.
Tuberculosis (TB), caused by Mycobacterium tuberculosis (Mtb), remains a significant global health challenge due to the emergence of drug-resistant strains. This study targets Flavin-dependent thymidylate synthase (ThyX), an essential enzyme in the thymidylate biosynthesis pathway crucial for bacterial DNA replication. We utilized advanced computational techniques, including molecular dynamics (MD) simulations and interaction energy analysis, to examine the binding interactions and stability of various thiazole-thiadiazole compounds with Mtb ThyX.
View Article and Find Full Text PDFThis study reports the synthesis, characterization, and biological evaluation of a series of pyrazolyl-thiazole derivatives of thiophene. Seven compounds were synthesized and characterized using NMR spectroscopy and mass spectrometry. The antimicrobial activities of these derivatives were evaluated against various bacterial (, , , ) and fungal strains (, , , ), demonstrating significant inhibition zones and low minimum inhibitory concentrations (MIC).
View Article and Find Full Text PDFTuberculosis remains a global health threat, with increasing infection rates and mortality despite existing anti-TB drugs. The present work focuses on the research findings regarding the development and evaluation of thiadiazole-linked thiazole derivatives as potential anti-tuberculosis agents. We present the synthesis data and confirm the compound structures using spectroscopic techniques.
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