PolyTherics Receives a Technology Strategy Board Grant to Develop Fusion Proteins
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PolyTherics Limited has announced that it has started work on a Technology Strategy Board (TSB) funded project to produce fusion proteins using its chemical linker technologies.
PolyTherics will chemically fuse different but complementary proteins using its proprietary polyethylene glycol (PEG) linkers. The goal of the project is to develop a way of fusing proteins that is both quicker and cheaper than producing a fusion protein using recombinant techniques whilst retaining the different functions of both proteins. This will allow for rapid generation of a range of new fusion proteins for screening for a range of uses in a variety of industries, including as potential therapeutic products.
As PolyTherics’ PEGylation technologies enable the PEG to be attached to a specific site on a protein, either on the histidine residues added to facilitate its purification, or at a naturally occurring disulfide, the effect of the PEG on the function of the protein can be minimized. In addition, PEG is known to protect proteins from breakdown by proteases and thus improve their stability, a potential advantage over recombinant fusion proteins.
PolyTherics will chemically fuse different but complementary proteins using its proprietary polyethylene glycol (PEG) linkers. The goal of the project is to develop a way of fusing proteins that is both quicker and cheaper than producing a fusion protein using recombinant techniques whilst retaining the different functions of both proteins. This will allow for rapid generation of a range of new fusion proteins for screening for a range of uses in a variety of industries, including as potential therapeutic products.
As PolyTherics’ PEGylation technologies enable the PEG to be attached to a specific site on a protein, either on the histidine residues added to facilitate its purification, or at a naturally occurring disulfide, the effect of the PEG on the function of the protein can be minimized. In addition, PEG is known to protect proteins from breakdown by proteases and thus improve their stability, a potential advantage over recombinant fusion proteins.
