Specific Adsorption of Histidine-Tagged Proteins on Silica Surfaces Modified with Ni<sup>2+</sup>/NTA-Derivatized Poly(ethylene glycol)

Kang, Eung Shick; Park, Jin-Won; McClellan, Scott J; Kim, Jong-Mok; Holland, David; G, Lee; Franses, Elias I.; Park, Kinam; Thompson, David H.

doi:10.1021/la063719e

Cited by 56 publications

(38 citation statements)

References 54 publications

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“…The addition of poly(ethyleneglycol) (PEG) increases protein capture efficiency (15, 16). Multivalent NTAs improve affinity by allowing multiple chelated nickels within the NTA cluster to interact with a single his-tag (6, 17–19).…”

Section: Introductionmentioning

confidence: 99%

Influence of Multivalent Nitrilotriacetic Acid Lipid−Ligand Affinity on the Circulation Half-Life in Mice of a Liposome-Attached His₆-Protein

et al. 2010

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Metal chelation-ligand interactions, such as occur between nitrilotriacetic acid (NTA)-nickel and multihistidines, enable the non-covalent attachment of histidine-modified proteins to liposomes and other particles. We compared three lipids: a mono-NTA lipid (circa 10 uM affinity) and two tris-NTA lipid derivatives (circa 3 nM and 0.2 nM affinity) in their ability to retain two different his6-containing proteins on NTA-liposomes in the presence of serum or plasma and after intravenous injection in mice. At nanomolar affinities the off-rate of a his6-ligand is sufficiently long so that his6-proteins attached to particle surfaces will remain with the particle for hours; thus, we hypothesized that the increased his6 affinity of multivalent NTA-modified liposomes would retain his6-proteins longer both in vitro and in vivo. For each of the three lipids, we found a robust association and complete activity retention of two his6-modified proteins: a far red-fluorescent protein, monomeric Katushka (mKate), and a prodrug-converting enzyme, yeast cytosine deaminase (yCD). Proteins associated more tightly in vitro with tris-NTA liposomes than with mono-NTA liposomes in the presence of refiltered fetal calf serum and mouse plasma. Free yCD exchanged with previously associated mKate for tris-NTA binding sites on the liposome surface. This exchange was due to the exchange of the proteins for NTA occupancy and not due to the exchange of tris-NTA lipid out of the liposome. The amount of yCD on the surface was similar if the proteins were co-associated or if mKate was pre-associated. This exchange confirms that NTA associated proteins are in a dynamic state and can exchange with multihistidine proteins in the biological milieu. There was no difference in circulation time of the protein when it was intravenously administered by itself or attached to any of the NTA-modified liposomes because in vivo the protein was rapidly released from the NTA liposomes. Upon recovery from blood, liposomes containing tris-NTA accumulated a different plasma protein profile than control liposomes, suggesting that Ni-NTA specifically interacts with some plasma proteins. The reason for the rapid protein dissociation from the liposome in vivo is not clear; it could be due to displacement by endogenous histidine-containing proteins or to natural chelators that remove nickel from the NTA. Regardless of the cause, improvements in chelator or ligand design are needed before metal chelation will be capable of retaining histidine-modified proteins on NTA liposomes after in vivo administration.

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Section: Introductionmentioning

confidence: 99%

Influence of Multivalent Nitrilotriacetic Acid Lipid−Ligand Affinity on the Circulation Half-Life in Mice of a Liposome-Attached His₆-Protein

et al. 2010

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“…Kröger et al (1999) developed a synthetic chelator thioalkane self-assembled on gold surface for the oriented and reversible immobilization of proteins via hexahistidine extensions. Kang et al (2007) presented the silica surfaces modified with NTA-PEG derivatives for immobilizing hexahistidine-tagged proteins. These literatures show that the affinity tag surfaces developed by NTA to form a quadridentate chelate offer superior specific affinity and stronger chelator/metal/His-tag interactions.…”

Section: Introductionmentioning

confidence: 99%

Protein microarray chip with Ni–Co alloy coated surface

Chang

2010

Biosensors and Bioelectronics

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“…Because NTA has been widely used in the purification and manipulation of His tagged proteins, such as surface immobilization, biosenser detection, and fluorescence labeling. [8][9][10][11][12][13][14][15][16][17] PEG modification, so-called PEGylation, 18 has been designed to increase the solubility and stability of protein as well as reduce the protein immunogenicity. Moreover, by preventing the rapid renal clearance of small proteins and their receptor-mediated uptake by the reticuloendothelial system, PEGylation can be effective in prolonging the plasma half-time.…”

Section: Introductionmentioning

confidence: 99%

Tumor Targeting of Protein Through Poly(ethylene glycol) Conjugation with Metal Coordination

Yoshida

Tabata²

2010

J. Nanosci. Nanotech.

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The objective of this study is to introduce a new and simple conjugation method of protein with poly(ethylene glycol) (PEG) based on metal coordination. A chelating residue N,N-bis(carboxymethyl)-L-lysine (NTA) was chemically introduced into one terminal of PEG with another terminal of methoxy group (MeO-PEG). Cu2+ or Zn2+ ions were chelated into the NTA residue of MeO-PEG-NTA prepared. Chromatographic experiments revealed that transferrin (Tf) was conjugated to the MeO-PEG-NTA based on Cu2+ ions coordination. The amount of PEG conjugated increased with an increase in that added. Fluorescently labeled Tf was conjugated by the MeO-PEG-NTA with Cu2+ or Zn2+ coordination and injected intravenously into tumor-bearing mice. The Tf conjugated with the MeO-PEG-NTA based on Cu2+ coordination was accumulated in the tumor site to a significantly great extent compared with the free Tf and Tf conjugated with the Zn2+ coordinated MeO-PEG-NTA. A body distribution assay with radiolabeled Tf demonstrated that PEG conjugation with Cu2+ coordination enabled Tf to prolong the blood circulation and enhance the tumor accumulation. When interferon (IFN) was conjugated with the Cu(2+)-coordinated MeO-PEG-NTA and subcutaneously injected into tumor-bearing mice, the in vivo tumor growth was significantly suppressed compared with the injection of free IFN and IFN conjugated by Zn(2+)-coordinated MeO-PEG-NTA. It is concluded that the Cu(2+)-coordinated PEG conjugation can modify the body distribution of protein only by simple mixing in aqueous solution. The PEG conjugation with metal coordination could increase the in vivo half-life period of proteins in the blood, and consequently enhance the accumulation amount at the tumor site.

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Specific Adsorption of Histidine-Tagged Proteins on Silica Surfaces Modified with Ni²⁺/NTA-Derivatized Poly(ethylene glycol)

Cited by 56 publications

References 54 publications

Influence of Multivalent Nitrilotriacetic Acid Lipid−Ligand Affinity on the Circulation Half-Life in Mice of a Liposome-Attached His₆-Protein

Influence of Multivalent Nitrilotriacetic Acid Lipid−Ligand Affinity on the Circulation Half-Life in Mice of a Liposome-Attached His₆-Protein

Protein microarray chip with Ni–Co alloy coated surface

Tumor Targeting of Protein Through Poly(ethylene glycol) Conjugation with Metal Coordination

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Specific Adsorption of Histidine-Tagged Proteins on Silica Surfaces Modified with Ni2+/NTA-Derivatized Poly(ethylene glycol)

Cited by 56 publications

References 54 publications

Influence of Multivalent Nitrilotriacetic Acid Lipid−Ligand Affinity on the Circulation Half-Life in Mice of a Liposome-Attached His6-Protein

Influence of Multivalent Nitrilotriacetic Acid Lipid−Ligand Affinity on the Circulation Half-Life in Mice of a Liposome-Attached His6-Protein

Protein microarray chip with Ni–Co alloy coated surface

Tumor Targeting of Protein Through Poly(ethylene glycol) Conjugation with Metal Coordination

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Product

Resources

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Specific Adsorption of Histidine-Tagged Proteins on Silica Surfaces Modified with Ni²⁺/NTA-Derivatized Poly(ethylene glycol)

Influence of Multivalent Nitrilotriacetic Acid Lipid−Ligand Affinity on the Circulation Half-Life in Mice of a Liposome-Attached His₆-Protein

Influence of Multivalent Nitrilotriacetic Acid Lipid−Ligand Affinity on the Circulation Half-Life in Mice of a Liposome-Attached His₆-Protein