Aggregation and supramolecular membrane interactions that influence anion transport in tryptophan-containing synthetic peptides.

摘要: Self-assembly is a desired property in supramolecular chemistry, but extensive aggregation may be counterproductive. Rigid systems typically have better organization, are inherently less dynamic. This work shows that ion transport by amphiphilic heptapeptides (synthetic anion transporters or SATs) affected of the monomers bulk aqueous phase to which they added and within bilayer. Ion was assessed for all compounds assay Cl(-) release from liposomes. The mechanism confirmed planar bilayer conductance studies two at opposite ends efficacy scale. Dynamic light scattering, Langmuir trough, transmission electron microscopy, liposomes, were used assess importance self-assembly versus transport. Generally, greater has an adverse effect on transport, although least dimerization required readily Cl(-). Anion these found sensitive changes C-terminal portion (Gly)(3)Pro(Gly)(3) sequence. Moreover, significant difference apparent when L-Trp replaced D-Trp same position.