Almac launches site-specific PEGylation technology
UK contract services specialist Almac has used its expertise in production and engineering of both recombinant proteins and synthetic peptides to develop a proprietary technology that overcomes issues inherent with other conjugation approaches.
UK contract services specialist Almac has used its expertise in production and engineering of both recombinant proteins and synthetic peptides to develop a proprietary technology that overcomes issues inherent with other conjugation approaches.
The site-specific ligation technology has been developed into an enabling and practical approach for site-specific PEGylation of recombinantly derived proteins.
Currently available PEGylation technologies produce products that are PEGylated at multiple sites in an uncontrolled manner. This inevitably results in a population of molecules PEGylated in locations that crowd the active centre or binding regions resulting in a net decrease in potency versus the un-PEGylated analogue.
The Almac approach enables homogeneous PEGylated populations where the specific PEGylation site can be selected and controlled, thus improving efficacy compared with existing PEGylation techniques, decreasing cost of goods and substance dosed to patient; while still providing improved ADME profile due to the addition of the PEG moiety.
In addition, for synthetic peptides and proteins, Almac has extensive expertise in the synthesis, engineering and labelling of polypeptides of up to 200 amino acids. Site specific PEGylation of synthetic folded polypeptides can be achieved using a generic methodology developed for the site-specific labelling of folded synthetic proteins in high yield.
"The application of our unique ligation technology to the field of half-life extension with site-specific PEGylation will enable our partners to benefit from Almac's state of the art peptide and protein engineering techniques for the improvement of their drug products," said Almac Sciences" president and managing director, Stephen Barr.
