Clinical chelation therapy compounds for mercury poisoning usually contain thiol moieties. Current chelation therapies administer dimercaptosuccinic acid (DMSA) and dimercaptopropanesulfonic acid (DMPS) as Hg2+ chelators.  To improve upon current therapies, this present study seeks to better understand the complexation interactions of mercury (II) with cysteine (-CH2-SH side chain) containing tetra-peptides. Density functional theory (DFT) calculations using the M06-2X/6-31G(d,p)/SDD level of theory have been conducted to investigate structural and thermodynamic aspects of the interactions of mercury (II) with these peptide ligands. To improve complexation energy values MP2/6-311G**(cc-pVDZ-PP) single-point energies are determined on all structures. All calculations are performed using the SMD solvation model. To optimize complexation between mercury (II) and the tetra-peptides, the two internal amino acids are varied. The primary focus here is placed on the tetra-peptides cys-gly-gly-cys, cys-glu-gly-cys, cys-gly-glu-cys, cys-glu-glu-cys, including their stereoisomers.

Computational study of complexes between mercury (II) and tetra-peptides with N- and C-terminal cysteine amino acids

245th National Meeting (2013)

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