We developed a protocol in which a mix of different molecular modeling techniques was used in an attempt to identify and predict the mechanism of allosteric inhibition of human peroxiredoxin (Prx).Inspired by experimental results,and in search of a potent inhibitor of Prx,we scanned the surface of human peroxiredoxin dimer to identify possible allosteric binding sites and employed molecular dynamics and docking to establish a plausible scenario of allosteric inhibition of Prxs function as a reducing agent for peroxide.