934367-84-7

Upstream product

• 75-15-0 carbon disulfide 
• 673-06-3 D-(R)-phenylalanine 
• 3926-62-3 sodium monochloroacetic acid 

Downstream Products

• 1416218-91-1 C₂₈H₂₀ClN₃O₃S₂ 
• 1416218-92-2 C₂₈H₁₉Cl₂N₃O₃S₂ 
• 1416218-93-3 C₃₀H₂₅N₃O₃S₂ 
• 1416218-94-4 C₂₉H₂₃N₃O₃S₂ 
• 1416218-95-5 C₂₈H₂₁N₃O₃S₂ 
• 1416218-96-6 C₂₈H₂₀BrN₃O₃S₂ 
• 1416218-97-7 C₂₈H₂₀FN₃O₃S₂ 
• 1416218-98-8 C₂₈H₂₀BrN₃O₃S₂ 
• 1416219-01-6 C₂₉H₂₃N₃O₄S₂ 
• 1416219-05-0 C₂₈H₂₀FN₃O₃S₂ 
• 1609466-54-7 (R,Z)-2-(5-(4-((benzyloxy)carbonyl)benzylidene)-4-oxo-2-thioxothiazolidin-3-yl)-3-phenylpropanoic acid 

Relevant academic research and scientific papers

Synthesis and biological evaluation of (E)-1-(substituted)-3-phenylprop-2-en-1-ones bearing rhodanines as potent anti-microbial agents

Herein, we report the design, syntheses and in vitro anti-microbial activity of two series of rhodanines with chalcone moiety. Anti-microbial tests showed that some of the synthesized compounds exhibited good inhibition (MIC=1-8μg/mL) against multi-drug-r

Discovery of 1,3-diphenyl-1H-pyrazole derivatives containing rhodanine-3-alkanoic acid groups as potential PTP1B inhibitors

Two series of 1,3-diphenyl-1H-pyrazole derivatives containing rhodanine-3-alkanoic acid groups were identified as competitive protein tyrosine phosphatase 1B (PTP1B) inhibitors. Among the compounds studied, IIIv was found to have the best in vitro inhibition activity against PTP1B (IC50 = 0.67 ± 0.09 μM) and the best selectivity (9-fold) between PTP1B and T-cell protein tyrosine phosphatase (TCPTP). Molecular docking studies demonstrated that compounds IIIm, IIIv and IVg could occupy simultaneously at both the catalytic site and the adjacent pTyr binding site. These results provide novel lead compounds for the design of inhibitors of PTP1B as well as other PTPs.

Design, synthesis, SAR and biological investigation of 3-(carboxymethyl)rhodanine and aminothiazole inhibitors of Mycobacterium tuberculosis Zmp1

Sixteen 3-(carboxymethyl)rhodanines, and twelve aminothiazoles as rhodanine-mimetics were designed, synthesized and tested as inhibitors of the Zmp1 enzyme from Mycobacterium tuberculosis (Mtb). Almost all rhodanines (5a–d, 5f–n, and 7a–b) exhibited Zmp1 inhibition with IC50 values in the range 1.3–43.9 μM, whereas only aminothiazoles 12b and 12d proved active with IC50 values of 41.3 and 35.7 μM, respectively. Structure-activity relationships (SAR) were coupled with molecular modeling studies to highlight structural determinants for Zmp1 inhibition. Moreover, rhodanines 5a and 5c induced 23.4 and 53.8% of Mtb growth inhibition in THP-1 infected cells, respectively, at the non-toxic concentration of 10 μg/ml. This work represents a step forward in targeting Zmp1 by small molecules.

Discovery of the first potent and selective Mycobacterium tuberculosis Zmp1 inhibitor

The Mycobacterium tuberculosis extracellular zinc metalloprotease 1 (Zmp1) has been proposed to play a key role in phagosome maturation and to enhance the survival of Mycobacterium tuberculosis in the host. Consequently, small molecule inhibitors of Zmp1