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2015 ; 16
(10
): 25831-64
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Site-Specific PEGylation of Therapeutic Proteins
#MMPMID26516849
Dozier JK
; Distefano MD
Int J Mol Sci
2015[Oct]; 16
(10
): 25831-64
PMID26516849
show ga
The use of proteins as therapeutics has a long history and is becoming ever more
common in modern medicine. While the number of protein-based drugs is growing
every year, significant problems still remain with their use. Among these
problems are rapid degradation and excretion from patients, thus requiring
frequent dosing, which in turn increases the chances for an immunological
response as well as increasing the cost of therapy. One of the main strategies to
alleviate these problems is to link a polyethylene glycol (PEG) group to the
protein of interest. This process, called PEGylation, has grown dramatically in
recent years resulting in several approved drugs. Installing a single PEG chain
at a defined site in a protein is challenging. Recently, there is has been
considerable research into various methods for the site-specific PEGylation of
proteins. This review seeks to summarize that work and provide background and
context for how site-specific PEGylation is performed. After introducing the
topic of site-specific PEGylation, recent developments using chemical methods are
described. That is followed by a more extensive discussion of bioorthogonal
reactions and enzymatic labeling.
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