• J. Inorg. Biochem. · Mar 2019

    Does phosphorylation increase the binding affinity of aluminum? A computational study on the aluminum interaction with serine and O-phosphoserine.

    • Elena Formoso, Rafael Grande-Aztatzi, and Xabier Lopez.
    • Farmazia Fakultatea, Euskal Herriko Unibertsitatea (UPV/EHU), 01006 Vitoria-Gasteiz, Euskadi, Spain; Donostia International Physics Centre (DIPC), Donostia 20018, Euskadi, Spain. Electronic address: elena.formoso@ehu.eus.
    • J. Inorg. Biochem. 2019 Mar 1; 192: 33-44.

    AbstractSeveral toxic effects arise from aluminum's presence in living systems, one of these effects is to alter the natural role of enzymes and non-enzyme proteins. Aluminum promotes the hyperphosphorylation of normal proteins. In order to assess the aluminum-binding abilities of phosphorylated proteins and peptides, the interaction of aluminum at different pH with serine and phosphoserine is studied by a Density Functional Theory study, combined with polarizable continuum models to account for bulk solvent effects, and the electronic structure of selected complexes are analyzed by Quantum Theory of "Atoms in Molecules". Our results confirm the high ability of aluminum to bind polypeptides as the pH lowers. Moreover, the phosphorylation of the building blocks increases the affinity for aluminum, in particular at physiological pH. Finally, aluminum shows a tendency to be chelated forming different size rings.Copyright © 2018 Elsevier Inc. All rights reserved.

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