First Insight into the Symmetry and Flexibility of Membrane Efflux Pump P‐Glycoprotein by Novel Bifunctional Modulators

Abstract

The other way round. The protein-target structure of P-glycoprotein is supposed to have an unexpectedly rigid symmetric binding region. Even the smallest deviations from symmetric inhibitor substitution lead to a decrease in inhibitory activity. However, the highest inhibitory activities shown towards HIV-1 protease are by asymmetric representatives, such as 1, thus demonstrating a high degree of flexibility of this protein-binding region.