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In this work we present and compare with experiments the results of extensive Molecular Dynamics simulations of model systems comprising an Aβ1-40 peptide in water in interaction with short peptides (β-sheet breakers) mimicking the 17-21 region of the Aβ1-40 sequence.Various systems differing in the customized β-sheet breaker structure have been studied.Specifically we have considered three kinds of β-sheet breakers, namely Ac-LPFFD-NH2 and two variants thereof, one obtained by substituting the acetyl group with the sulfonic amino acid taurine (Tau-LPFFD-NH2) and a second, novel one in which the aspartic acid is substituted by an asparagine (Ac-LPFFN-NH2).Thioflavin T fluorescence, Circular Dichroism and Mass Spectrometry experiments have been performed indicating that β-sheet breakers are able to inhibit in vitro fibril formation and prevent the β-sheet folding of portions of the Aβ1-40 peptide.