Metal-free affinity media/agents for the selective capture of histidine-rich peptide sequences
The present invention is compatible with a broad range of peptides and proteins, and does not destroy the function of the protein of peptide during the purification process. Additionally, the present invention is less expensive than comparable biomacromolecule-based affinity media/agents.
Media/agents can be used in the industry and academic research contexts, for example, for the selective purification of chemically or biologically produced peptides and proteins that contain histidine-rich sequences.
The ability to selectively purify proteins and peptides is a critical tool for academic and industrial research laboratories. For example, purification of monoclonal antibodies (a protein) is one of the most important processes in monoclonal antibody drug development. Yet, existing processes used by labs to purify proteins and peptides suffer from at least one of three significant drawbacks: (1) it may be costly to produce, (2) it may have damaging effects to peptides and proteins containing metals as essential components for their functions, and (3) it may have poor durability. In one existing process, fusion of histidine-rich sequences to peptides and proteins has been applied to assist the purification of peptides and proteins by using metal ion immobilized affinity media/agents. However, metal ion immobilized affinity media/agents may exchange or extract the essential metallic components in the peptide and protein, thereby damaging the peptide or protein. In another existing process, biomacromolecule-based affinity media/agents, including antibodies have also been developed for the capture of histidine-rich sequences. However, biomacromolecule-based affinity media/agents suffer from poor durability and high cost of production. The present invention utilizes metal-free synthetic polymer-based materials for the purification of peptides and proteins containing or being fused with histidine-right sequences that do not damage the function of the protein and is comparably less expensive to produce. Desired binding affinity is accomplished by using hydrophobic and anionic carboxyl groups as the basis for the interaction, rather than metal-histidine side chain chelation.
Limitations The present invention is not compatible with all proteins or peptides. Additionally, hydrophobic and anionic carboxyl groups as a basis of the interaction between the media/agent and the target protein may be weaker than metal-histidine chelation of competing technologies. State Of Development The inventors are working on a prototype. Tech ID/UC Case 27397/2015-519-0 Related Cases 2015-519-0
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