Facile Synthesis of Nickel Chelate Polyacrylamide of use as Affinity Capture Media
Additional Funding Sources
The project described was supported by the University of idaho under Grant No. ACX012.
Presentation Date
7-2018
Abstract
We created a nickel chelate polymer that allows for the purification of histidine tagged recombinant proteins. A histidine tag is a genetic modification that places a string of histidine residues on the N or C terminus of a protein that allows for the protein to be purified by means of affinity capture. A metal bearing media is required to purify the proteins tagged with these histidine residues. Currently, there is not a facile method to produce a polymer that can purify proteins like this via an affinity capture process. We developed a synthetic method for creation of a polymer decorated with nickel. Our polymer captures these proteins using this affinity capture process. We used Green Fluorescent Protein modified to contain these histidine tags to test our polymer. Using florescence, we tracked the location of the protein throughout the affinity capture and elution process and characterized the performance of our polymer for yield and purity.
Facile Synthesis of Nickel Chelate Polyacrylamide of use as Affinity Capture Media
We created a nickel chelate polymer that allows for the purification of histidine tagged recombinant proteins. A histidine tag is a genetic modification that places a string of histidine residues on the N or C terminus of a protein that allows for the protein to be purified by means of affinity capture. A metal bearing media is required to purify the proteins tagged with these histidine residues. Currently, there is not a facile method to produce a polymer that can purify proteins like this via an affinity capture process. We developed a synthetic method for creation of a polymer decorated with nickel. Our polymer captures these proteins using this affinity capture process. We used Green Fluorescent Protein modified to contain these histidine tags to test our polymer. Using florescence, we tracked the location of the protein throughout the affinity capture and elution process and characterized the performance of our polymer for yield and purity.
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