Alzheimer's disease, a severe neurodegenerative disorder, is believed to be caused by the interneuronal aggregation of the amyloid β peptide. It has no cure yet. Despite rigorous research, the mechanism of aggregation is not yet fully delineated. Especially probing the early events of the aggregation is difficult as we have no control on the kinetics of the process of aggregation. We have used amyloid β derived switch-peptides that behave as the functional mimic of the amyloid β peptide, and demonstrated that side chain aromatic interactions precede the β-sheet formation resulting in fibrillization. Detailed investigation into the early events of aggregation has become possible as the kinetics of aggregation of the switch-peptides can be controlled. We have used ultraviolet (UV) spectroscopy, circular dichroism (CD), Raman spectroscopy and Molecular Dynamics (MD) simulation as a combined experimental and theoretical approach.