HIV capsid is formed by a single viral protein (CA), which plays an essential role in early as well as later steps of infection1. The correct capsid assembly is essential for HIV infectivity2. The high conservation of the aminoacidic sequence of CA and its high sensitivity to mutations highlights its role in the viral cycle success and supports the research of molecules able to interfere with CA multimerization as possible HIV inhibitors3. In this work we studied 84 compounds selected through a massive virtual screening of molecules capable of interacting with a conserved region of the interface surface between CA monomers. We analyzed the in vitro assembly of recombinant CA in the presence of these compounds, identifying 30 molecules affecting its multimerization. Additionally, using an in cellulo HIV infection model, we identified 4 compounds interfering with viral infection with IC50 values between 3 and 13 μM.