ABSTRACT The interaction between three divalent cations (Pb2+, Zn2+ and Cd2+) and a sequence of 12 amino-acids (DKNGDGEVSFEE) corresponding to the second binding site of Calbindin D9K, a calcium binding protein, is evaluated, as well as the conformation that this peptide can adopt due to the coordination. Equilibrium studies are performed through potentiometry and structural studies through NMR. The lead derivative shows the highest similarity to the standard conformation of the calcium-loaded site in the protein, which seems to clarify why this protein is the pathway for lead intake.
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