On the Function and Structure of Synthetically Modified Porins

摘要

The attachment of synthetic modulators to biological ion channels is promising for applications in neurobiology and sensing.While progress has been made on the modification of channels with a narrow ion conductance pathway,the use of wider pores for ion-channel engineering has been mainly limited to hemolysin.The porins offer a broad variety of β-barrel architectures with pores of variable diameters, which makes them promising candidates for attaching synthetic modulators. Unlike the oligomeric hemolysins, porins have a conductance pathway formed by a single polypeptide chain, which eases synthetic modifications in the pore interior. Herein we present functional and structural data for the implementation of synthetic modulators into the trimeric porin OmpF.