The misfolding and aggregation of β-amyloid peptides (Aβ) into amyloid fibrils, a process that has been pathologically linked to the onset of Alzheimer's disease, is dependent on the presence of a heterogeneous surface (e.g., cell membrane). Understanding of the kinetics of amyloid fibril formation and associated structural transition from monomers to intermediates and eventually to fibrils is critical for the development of viable therapeutic agents. In this work, using circular dichroism (CD), atomic force microscopy (AFM), surface plasmon resonance (SPR), and molecular dynamics (MD) simulations, we studied the adsorption, aggregation, and conformational changes of Aβ_1–42 from fresh monomers to fully grown fibrils on four model self-assembled monolayers (SAMs): hydrophobic CH₃-terminated SAM, hydrophilic OH-terminated SAM, negatively charged COOH-terminated SAMs, and positively charged NH₂-terminated SAM. The seeding effect of Aβ_1–42 on the kinetics of Aβ aggregation on different SAMs is also examined. The CD, AFM, and SPR data show that all of these SAMs greatly accelerate the formation of β-sheets and amyloid fibrils through surface-enhanced interactions, but Aβ_1–42peptides preferentially adsorb on a hydrophobic CH₃-SAM and a positively charged NH₂-SAM with much stronger interactions than on a hydrophilic OH-SAM and a negatively charged COOH-SAM. MD simulations further reveal that hydrophobic interactions present a general driving force for Aβ adsorption on all SAMs. As Aβ aggregates grow into larger species by packing hydrophobic C-terminals to form a hydrophobic core while exposing hydrophilic and negatively charged N-terminals to solution, electrostatic interactions become more strengthened when they interact with the SAMs especially for the COOH-SAM and the NH₂-SAM. Thus, both hydrophobic and electrostatic interactions contribute differently to different Aβ–SAM systems and to different aggregation stages. A postulated mechanism is proposed to describe the structure and kinetics of Aβ aggregation from aqueous solution to the SAMs, providing valuable insights into Aβ aggregation on biological cell membranes.