alexa Coordination of Two High-Affinity Hexamer Peptides to Copper(II) and Palladium(II) Models of the Peptide−Metal Chelation Site on IMAC Resins
Microbiology

Microbiology

Journal of Chemical Biology & Therapeutics

Author(s): Chen Y, Pasquinelli R, Ataai M, Koepsel R, Kortes A, Shepherd RE

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Complexes of Ser-Pro-His-His-Gly-Gly and (His)6 with [PdII(mida)(D2O)] and [CuII(mida)(H2O)2] (mida2- = N-methyliminodiacetate) have been studied by 1H NMR and EPR, respectively, as models for binding of protein separation tags on immobilized metal ion affinity chromatography (IMAC) sites. Peptide attachment in the [MII(mida)(peptide)] complexes occurs via the N-terminal amine or histidyl donor and third and fourth histidyl donors. Proline in the second position of the peptide chain improves molecular mechanics and bond angles for coordination.

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This article was published in J InorgChem and referenced in Journal of Chemical Biology & Therapeutics

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