Diazobenzenesulfonic acid is a whiter or reddish crystalline acid derivative of sulfanilic acid. It is a desensitizer (inhibitor) of allosteric effect for myosin ATPase 13.
QAQ dichloride is a photoswitchable compound that blocks voltage-gated Na v and K v channels. Its channel-blocking activity is observed in the trans form of the azobenzene photoswitch, while the cis form does not exhibit this effect. This compound is membrane-impermeant and selectively enters pain-sensing neurons expressing endogenous import channels. QAQ dichloride functions as a light-sensitive analgesic and provides a valuable tool for investigating signaling mechanisms involved in acute and chronic pain [1] [2].
Photoswitchable PAD inhibitor is a photoactivated protein arginine deiminase (PAD) inhibitor and a derivative of BB-Cl-amidine that contains an azobenzene photoswitch allowing optical control of PAD activity.1 Without photoactivation, it is a weak inhibitor of PAD2 (IC50 = >100 μM) and is less potent than BB-Cl-amidine in inhibiting citrulline production in vitro (kinact KIs = 2,300, 600, 1,000, and 10,510 M-1min-1 for PAD1-4, respectively) and does not inhibit histone H3 citrullination in HEK293T cells overexpressing PAD2 when used at concentrations up to 100 μM. However, it can rapidly be photoactivated with UV-A radiation to the more active cis-isomer, which is an irreversible, competitive inhibitor of histone H3 citrullination with an IC50 value of 9.1 μM.References1. Mondal, S., Parelkar, S.S., Nagar, M., et al. Photochemical control of protein arginine deiminase (PAD) activity. ACS Chem. Biol. 13(4), 1057-1065 (2018). Photoswitchable PAD inhibitor is a photoactivated protein arginine deiminase (PAD) inhibitor and a derivative of BB-Cl-amidine that contains an azobenzene photoswitch allowing optical control of PAD activity.1 Without photoactivation, it is a weak inhibitor of PAD2 (IC50 = >100 μM) and is less potent than BB-Cl-amidine in inhibiting citrulline production in vitro (kinact KIs = 2,300, 600, 1,000, and 10,510 M-1min-1 for PAD1-4, respectively) and does not inhibit histone H3 citrullination in HEK293T cells overexpressing PAD2 when used at concentrations up to 100 μM. However, it can rapidly be photoactivated with UV-A radiation to the more active cis-isomer, which is an irreversible, competitive inhibitor of histone H3 citrullination with an IC50 value of 9.1 μM. References1. Mondal, S., Parelkar, S.S., Nagar, M., et al. Photochemical control of protein arginine deiminase (PAD) activity. ACS Chem. Biol. 13(4), 1057-1065 (2018).