The tripartite anthrax toxin from Bacillus anthracis represents the prototype of A-B type of toxins, where the effector A (an enzymatic subunit) is transported with the help of a binding component B into a target cell. Anthrax toxin consists of three different molecules, two effectors, lethal factor (LF) and edema factor (EF) and the binding component also known as protective antigen (PA). PA forms heptamers or octamers following binding to host cell’s receptors and mediates the translocation of the effectors into the cytosol via the endosomal pathway. The cation-selective PA63-channel is able to reconstitute in lipid membranes and can be blocked by chloroquine and other heterocyclic compounds. This suggests that the PA63-channel contains a binding site for quinolines. In this study, we investigated the structure-function relationship of different quinolines for the block of the PA63-channel. The affinity of the different chloroquine analogues to the PA63-channel as provided by the equilibrium dissociation constant was measured using titrations. Some quinolines had a much higher affinity to the PA63-channel than chloroquine itself. We also performed ligand-induced current noise measurements using fast Fourier transformation to get insight in the kinetics of the binding of some quinolines to the PA63-channel. The on-rate constants of ligand binding were around 108 M-1·s-1 at 150 mM KCl and were only little dependent on the individual quinoline. The off-rates varied between 4 s-1 and 160 s-1 and depended much more on the structure of the molecules than the on-rate constants. The possible use of the 4-aminoquinolines as a therapy is discussed.