Coordination of the six-mer peptide Gly-His-Pro-His-His-Gly to CuII and PdII N-methyliminodiacetate complexes as IMAC chelation site models

Copper(II), nickel(II) and zinc(II) complexes of N-acetyl-His-Pro-His-His-NH2: Equilibria, solution structure and enzyme mimicking

“…The large separation of pK 101 and pK [1][2][3][4][5][6][7][8][9][10][11] , and the small change in the Vis, CD and EPR spectra of the CuH À2 L species compared to [CuH À1 L] + indicates the formation of a mixed hydroxo ligand complex with {N im , N À amide , N im , OH À ) type coordination (Scheme 1). The pK 1-11 for the [CuH À1 L] + = CuH À1 L(OH) + H + process is 8.26, that is one unit lower, than e.g.…”

“…doi:10.1016/j.jinorgbio.2008.01.006 their surface [5][6][7]. Moreover, H and H/P-rich sequences like hexahistidine or GHPHHG have been playing important role in anchoring and purifying proteins on metal ionaffinity chromatography [8][9][10].…”

Comparison of Energy-Minimized Structures of [PdII(N-methyliminodiacetate)] Complexes of X1-His-X3-His-His Peptides as an Analysis of Steric and Specific Interactions with Synthetic Binding Tags for IMAC Separations

“…It was shown that the carboxylate donors from the mida 2-portion of the molecule are displaced as the peptide chain establishes a three-point contact via the remaining square-planar coordination positions of the Pd II center as shown in the figure for the Ser-Pro-His-His-Gly-Gly peptide (SPH-HGG) (9). EPR spectra of the Cu II analogue, [Cu II (mida)-(peptide)], confirm a similar structure for the Cu II -ida IMAC site models (9,10). A molecular mechanics calculation for the structure of the shorter SPHHG peptide complex, [Pd II (mida)(SPHHG)], which is related to the pentapetides of the present study, was carried out by the Spartan program using the MMFF94 force field.…”

“…A commonly used IMAC column has Cu II , Ni II , or Zn II sites supported by iminodiacetate chelation that is attached to a resin support (1)(2)(3). [Pd II (mida)(peptide)] complexes, mida 2-) N-methyliminodiacetate, have been useful for NMR purposes in modeling the coordination of peptides to IMAC binding sites (9,10). It was shown that the carboxylate donors from the mida 2-portion of the molecule are displaced as the peptide chain establishes a three-point contact via the remaining square-planar coordination positions of the Pd II center as shown in the figure for the Ser-Pro-His-His-Gly-Gly peptide (SPH-HGG) (9).…”

Electrochemical preparation of junction between a molecule and solid surface through a metal coordinative peptidic tag

“…The ECtag tagged model molecule is comprised of three domains as described in the following and as shown in Fig. 2: (1) an ECtag domain, designed to form a complex with transition-metal ions (and in this study, a typical coordinative peptide sequence was employed: HHHHHH [14][15][16][17][18]); (2) a polyethylene glycol (PEG) domain, employed to avoid molecular aggregation and unspecific adsorption to the substrate; (3) an FITC label domain. The designed model molecule is henceforth referred to as "ECtag-PEG" or "ECtag-PEG-FITC", according to the case.…”