Intermolecular interactions of gramicidin A' transmembrane channels incorporated into lysophosphatidylcholine lipid systems.

Fluorescence studies are reported on gramicidin A' incorporated into lysophosphatidylcholine phospholipid structures. The shift in the emission maximum during incorporation and the quenching of fluorescence by I- and by acrylamide of the incorporated state obtained after prolonged heating are consistent with the presence of the channel state comprised of two single-stranded beta 6 -helices associated head-to-head (formyl end-to-formyl end). The quantum yield for the incorporated state, when gramicidin A' is within the lipid matrix, is very low and indicates the occurrence of intermolecular Trp-Trp interactions. Possible interactions between channels within the lipid matrix are discussed utilizing Trp-Trp contacts.