The sequential adsorption of two proteins of the same or of an unlike nature on a heterogeneous hydrophobic surface is investigated through atomistic molecular dynamics simulations. By modeling two real protein fragments having a different secondary structure (alpha-helices or beta-sheets) on a graphite surface, the pre-adsorbed polypeptides are shown to modify the hydropathy of this substrate. Therefore, the graphite surface modified by the first adsorbed protein becomes more similar to a hydrophilic one in terms of both the interaction energy and the size of the second protein after the possible surface spreading.
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