Nickel‐Ion‐Mediated Control of the Stoichiometry of His‐Tagged Protein/Nanoparticle Interactions
Open Access
- 3 February 2009
- journal article
- research article
- Published by Wiley in Macromolecular Bioscience
- Vol. 9 (2) , 174-178
- https://doi.org/10.1002/mabi.200800289
Abstract
The interaction between synthetic materials and biomolecules plays an important role in biomedical and pathological sciences. An important issue in these interactions is control of stoichiometry. The interaction between NTA ligands and proteins with six consecutive His residues has been widely used for protein purification. Control of stoichiometry is an important issue in applying this recognition strategy to the creation of defined nanoparticle‐protein conjugates. In this communication we report the direct control of particle‐protein stoichiometry through variation of nickel chloride concentration, as demonstrated through fluorescence and gel electrophoresis. magnified imageKeywords
This publication has 23 references indexed in Scilit:
- Dual-Mode Fluorophore-Doped Nickel Nitrilotriacetic Acid-Modified Silica Nanoparticles Combine Histidine-Tagged Protein Purification with Site-Specific Fluorophore LabelingJournal of the American Chemical Society, 2007
- Kinetics of Metal-Affinity Driven Self-Assembly between Proteins or Peptides and CdSe−ZnS Quantum DotsThe Journal of Physical Chemistry C, 2007
- Assembly of Nanoparticle–Protein Binding Complexes: From Monomers to Ordered ArraysAngewandte Chemie International Edition in English, 2007
- Highly-Efficient Purification of Native Polyhistidine-Tagged Proteins by Multivalent NTA-Modified Magnetic NanoparticlesBioconjugate Chemistry, 2007
- Magnetic Nanoparticles: Synthesis, Protection, Functionalization, and ApplicationAngewandte Chemie International Edition in English, 2007
- Preparation and Characterization of Nickel Nanoparticles for Binding to His-tag Proteins and AntigensPharmaceutical Research, 2006
- Functionalization of Thioctic Acid-Capped Gold Nanoparticles for Specific Immobilization of Histidine-Tagged ProteinsJournal of the American Chemical Society, 2005
- Nitrilotriacetic Acid-Modified Magnetic Nanoparticles as a General Agent to Bind Histidine-Tagged ProteinsJournal of the American Chemical Society, 2004
- Localisation of the PsbH subunit in photosystem II: a new approach using labelling of his-tags with a Ni2+-NTA gold cluster and single particle analysisJournal of Molecular Biology, 2001
- Poly(Ethylene Glycol) ChemistryPublished by Springer Nature ,1992