In Alzheimer's disease (AD), amyloid β-protein (Aβ) self-assembles into toxic oligomers. Of the two predominant Aβ alloforms, Aβ 1–40 and Aβ 1–42 , the latter is particularly strongly linked to AD. N-terminally truncated and pyroglutamated Aβ peptides were recently shown to seed Aβ aggregation and contribute significantly to Aβ-mediated toxicity, yet their folding and assembly were not explored computationally. Discrete molecular dynamics approach previously captured in vitro-derived distinct Aβ 1–40 and Aβ 1–42 oligomer size distributions and predicted that the more toxic Aβ 1–42 oligomers had more flexible and solvent-exposed N-termini than Aβ 1–40 oligomers. Here, we examined oligomer formation of Aβ 3–40 , Aβ 3–42 , Aβ 11–40 , and Aβ 11–42 by the discrete molecular dynamics approach. The four N-terminally truncated peptides showed increased oligomerization propensity relative to the full-length peptides, consistent with in vitro findings. Conformations formed by Aβ 3–40/42 had significantly more flexible and solvent-exposed N-termini than Aβ 1–40/42 conformations. In contrast, in Aβ 11–40/42 conformations, the N-termini formed more contacts and were less accessible to the solvent. The compactness of the Aβ 11–40/42 conformations was in part facilitated by Val12. Two single amino acid substitutions that reduced and abolished hydrophobicity at position 12, respectively, resulted in a proportionally increased structural variability. Our results suggest that Aβ 11–40 and Aβ 11–42 oligomers might be less toxic than Aβ 1–40 and Aβ 1–42 oligomers and offer a plausible explanation for the experimentally observed increased toxicity of Aβ 3–40 and Aβ 3–42 and their pyroglutamated forms.