All 13 PH domains cause a degree of local clustering of PIP molecules upon binding to the membrane.
Highest titers were observed with one particular DARPin binding to the membrane distal domain of HER2/neu with medium affinity.
Upon binding to the membrane, a structural element in perfringolysin O moves to expose the edge of a previously hidden β-strand that forms the monomer-monomer interface and is required for oligomer assembly.
Biophysical studies have shown that this peptide is unstructured in solution, forms an antiparallel dimer of amphipathic helices upon binding to the membrane, and disrupts membrane via toroidal-type pore formation.
This ability is derived from the strength of molecular binding to the membrane interface as well as from the cohesiveness of the membrane itself.
A simple model is introduced where the binding to the membrane and the work for displacing the membrane lipids and creating a vacancy for the binding molecules determine the outcome of the event.
Homogenate binding assays on sheep brown fat demonstrated that the radioligand was binding to the membrane fraction and that the specific binding was not due to a lipophilic interaction between 125I-rat ANF and brown fat.
Accordingly, Munc18 protein levels and its binding to the membrane through its interaction with syntaxin1 influence the docking process [18], [19], [20], [21], [22].
