CAB7-3 is an orally effective HBV capsid assembly modulator that demonstrates excellent antiviral potency. It inhibits HBVDNA with an EC50 of 70 nM and has a CC50 of 32.3 μM. The compound exhibits significant anti-HBV activity across various cell models, with EC50 values of 70 μM in HBV-integrated HepDES19 cells, 1 nM in tetracycline-induced HepAD38 cells, and 2 nM in HBV-infected HLCZ01 cells. In vivo, CAB7-3 effectively reduces hepatic HBV core protein levels and suppresses viral replication. It shows good drug-like properties and safety, making it suitable for hepatitis B virus research.

CAB7-3 exhibits antiviral activity across multiple cell models, with a range of 0.001-1 μM over 6 days. In HepAD38 cells, it shows an EC50 of 1 nM, a CC50 of 26.54 μM, and a selectivity index (SI) of 26540; in HepDES19 cells, EC50 is 7 nM, CC50 is 32 μM, and SI is 481; and for HBV-infected HLCZ01 cells, EC50 is 2 nM, CC50 is 30.73 μM, and SI is 15365. CAB7-3 (0.0003-1 μM, 6 days) blocks new cccDNA formation in HepAD38 and HLCZ01 cells without affecting HBsAg secretion from existing cccDNA. Additionally, CAB7-3 (0.006-4 μM, 3 days) induces HBV core protein degradation and disrupts capsid assembly in HepG2 cells. In human liver microsomes, CAB7-3 (1 μM, 0-60 minutes) has a metabolic stability with a half-life (T1/2) of 169 minutes, an intrinsic microsomal clearance (CLint(mic)) of 8.2 μL/min/mg, an intrinsic liver clearance (CLint(liver)) of 7.4 mL/min/kg, and a remaining amount of 78.0% after 60 minutes. CAB7-3 (10 μM) does not induce CYP3A4 expression in human primary hepatocytes. CAB7-3 (0.3-100 μM) shows significantly lower hERG channel inhibition in HEK293 cells expressing hERG channels, with inhibition rates of 3.52%, 14.59%, 31.84%, 61.05%, 83.05%, and 94.76% at concentrations of 0.3, 1, 3, 10, 30, and 100 μM, respectively.

In a mouse model carrying HBV, CAB7-3 (administered orally at a dose of 15 mg/kg once daily for 18 consecutive days) suppresses the secretion of viral DNA-containing particles by inhibiting HBV capsid assembly.