We used HyperChem 7.0 and Spartan molecular mechanics software to examine the binding of a series of actinide ions to oxytocin, a model peptide.  Minimized energies, dipole moments, and symmetry elements were calculated for actinide ion binding to oxygen and nitrogen-containing side chains of the nine amino acid sequence of the model peptide. Results from our studies will be compared to experimental studies of actinide ion binding to the iron-transport protein, transferrin.  Our model study provides a theoretical template on which to build future studies of actinide ion binding to peptides and proteins.

Molecular mechanics study of the binding of Th(IV), Pa(V), U(VI), Np(V), Pu(IV), Am(III), and Ac(III) to a model peptide

242nd National Meeting (2011)

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