One influential parameter which mediates interactions between many types of molecules and biological membranes stems from the lumped contributions of the transmembrane potential, dipole potential and the difference in the surface potentials on both sides of a membrane. With relevance to cell physiology, such electrical features of a biomembrane are prone to undergoing changes as a result of interactions with the aqueous surrounding. Among the most useful tools devoted to exploring changes of electrical parameters of a lipid membrane induced by certain extracellular ions, lipid composition, and embedded membrane peptides and proteins, are spectroscopic imaging and the inner field compensation (IFC) method. In this work we layout the principles of a fully computerized version of the IFC method, which makes it more readily available to users. As a direct application, we deployed this improved version of the IFC method to time-resolve changes induced by alamethicin monomers upon membrane dipole potential, following their aggregation within an artificial lipid membrane. Intriguingly, even prior crossing the membrane core, the membrane-bound alamethicin monomers are shown to significantly increase the dipole potential of the monolayer they reside in. Such data further emphasize the yet less-explored interplay between membrane-based protein and peptides, and the membrane dipole potential.