<p>The replication cycle of many viruses involves a group of proteins called viroporins, whose general function is to increase membrane permeability. This function is achieved primarily by their self-oligomerization to form transmembrane channels that transport small ions or molecules across the lipid bilayer of enveloped viruses or host cell membrane. Viroporins are vital for viral replication; damage or deletion of the gene encoding the corresponding protein results in reduced or absent virulence. Viroporins are convenient targets for drug development due to their small size, which allows their structure to be easily determined by both experimental and computational methods of medicinal chemistry. The review summarizes the results of studies devoted to the use of viroporins as targets in the search for new small molecule inhibitors.</p>