HC102A 

HC102A is an Antibacterial agent and an inhibitor of DosS and DosT histidine sensor kinases, with an IC₅₀ of 1.9 μM against Mycobacterium tuberculosis DosS. HC102A does not alter the heme redox state of sensor kinases. HC102A reduces triacylglycerol synthesis and accumulation, decreases the survival rate of Mtb under non-replicating persistent and hypoxic conditions, and enhances the sensitivity of Mtb to Isoniazid (HY-B0329). HC102A can be used in research related to tuberculosis^[1][2][3].

HC102A (0.01-100 μM) potently and selectively inhibits DosR-dependent GFP fluorescence in Mtb CDC1551 (hspX′::GFP), with an EC₅₀ of 12.4 μM^[1].
HC102A (40 μM; 6 days) reduces TAG accumulation by 67% in Mtb CDC1551, thereby disrupting a key lipid metabolic process associated with persistence^[1].
HC102A (1-100 μM; 10 days) reduces the survival rates of Mtb CDC1551 and Erdman strains in a dose-dependent manner under hypoxic NRP conditions, and decreases the strain survival rate by approximately 50% at a dose of 10 μM^[1].
HC102A (1 h) directly inhibits autophosphorylation of purified Mtb DosS protein with an IC₅₀ of 1.9 μM, but has minimal effect on autophosphorylation of DosT^[1].
HC102A directly inhibits the autophosphorylation activity of the Mycobacterium tuberculosis DosS sensor kinase, but exerts no such effect on the DosT sensor kinase^[2].
HC102A inhibits the autokinase activity of DosS and DosT histidine kinases in *Mycobacterium tuberculosis*, reduces the hypoxia-induced survival rate of *Mycobacterium tuberculosis*, and exhibits extremely low cytotoxicity against mammalian cell lines^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

210.28

C₁₁H₁₈N₂O₂

91216-38-5

O=C1NC(=O)C2(N1)CC(C)CC(C)(C)C2

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Zheng H, et al. Inhibitors of Mycobacterium tuberculosis DosRST signaling and persistence. Nature chemical biology. 2017 Feb;13(2):218-225.  [Content Brief]

  [2]. Johnson BK, et al. Small Molecules That Sabotage Bacterial Virulence. Trends in pharmacological sciences. 2017 Apr;38(4):339-362.  [Content Brief]

  [3]. Stupar M, et al. Two-component sensor histidine kinases of Mycobacterium tuberculosis: Beacons for niche navigation. Molecular microbiology. 2022 May;117(5):973-985.  [Content Brief]