Custom Pegylation

PEG has great biocompatibility and can increase residence time of a variety of proteins/peptides. One of Akina’s custom synthesis options is coupling of PEG or other stabilizing agents to the protein/peptide of your choice. Contact John Garner (jg@akinainc.com) to learn how Akina can help you increase your peptides residence time.

The below article discusses the usage of pegylation to increase the residence time of a model BSA peptide. Go to the link below or to the original source for full-text for the article. (note the below article did not not necessarily use an Akina product for this research). Abstract follows:

"Methoxypolyethylene glycols of 1900 and 5000 daltons have been attached covalently to bovine serum albumin using cyanuric chloride as the coupling agent. When sufficient polymer is attached, the modified bovine serum albumin appears to lose its immunogenicity in the rabbit and, on intramuscular or intravenous injection, elicits antibodies neither to itself nor to native bovine serum albumin. It does not react with antibodies raised against native bovine serum albumin. Bovine serum albumin to which methoxypolyethylene glycol has been attached exhibits a blood circulating life in the rabbit rather similar to native bovine serum albumin, except that it is not removed from circulation by the eventual development of antibodies. Modified bovine serum albumins which had been iodinated with 125I, or prepared with [14C]cyanuric chloride, were injected intravenously in rabbits. Both labels appeared almost quantitatively in the urine after 30 days. The modified bovine serum albumins showed substantial changes in properties, such as solubility, electrophoretic mobility in acrylamide gel, ion exchange chromatography, and sedimentation, as compared with the unmodified protein."

A. Abuchowski, T. van Es, N.C. Palczuk, F.F. Davis, Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. Journal of Biological Chemistry 252(11) (1977) 3578-3581.

Full-Text: http://www.jbc.org/content/252/11/3578.full.pdf+html