Peptide self-assembly is a common phenomenon and plays important roles in physiological processes. An obvious example is β-amyloid (Aβ) peptides which can self-assemble to make up of long, insoluble ordered fibers, the main constituent of amyloid plaques in the brains of Alzheimer's disease patients. Studies revealed that sphere peptide units (PUs) with energy-rational structures formed at the initial self-assembling process driven mainly by the hydrophobic forces. With equal number of negative (K) and positive (E) charges distributing on the surface of the PUs, peptide clusters acted as the fundamental assembling units to elongate the cylindroid structures governed by electrostatic attraction. Controlling peptide self-assembly represents a new means to tune the stability and biological properties of peptides.