Abstract
Protein dimerization is a crucial biological process in which proteins interact into homo- or heterodimers to form a functional assembly. Understanding and modulating the molecular mechanisms of protein dimerization and their function represent the cutting edge of research and provide multiple entries for biomedical applications. Label-free methods sensitive to homodimer formation are still required. Electrochemical methods are sensitive to small structural changes due to the presence of a surface and polarization to high negative/positive potentials, where partial denaturation/unfolding can appear. Since the dimeric structure is usually more flexible, the electric field effects induce more salient structural changes close to the electrode surface, accompanied by higher chronopotentiometric/voltammetric responses. Serum albumin and anterior gradient receptor-2 were studied as model homodimeric proteins.