Nature Biotechnology
- 24, 1241 - 1252 (2006)
Published online: 10 October 2006; | doi:10.1038/nbt1252
Post-translational modifications in the context of therapeutic proteinsGary Walsh1 & Roy Jefferis21
Industrial Biochemistry Program, University of Limerick, Castletroy, Limerick City, Ireland. 2
The Division of Immunity & Infection, University of Birmingham B15 2TT, United Kingdom.
Correspondence should be addressed to Gary Walsh Gary.walsh@ul.ie The majority of protein-based biopharmaceuticals approved or in clinical trials bear some form of post-translational modification (PTM), which can profoundly affect protein properties relevant to their therapeutic application. Whereas glycosylation represents the most common modification, additional PTMs, including carboxylation, hydroxylation, sulfation and amidation, are characteristic of some products. The relationship between structure and function is understood for many PTMs but remains incomplete for others, particularly in the case of complex PTMs, such as glycosylation. A better understanding of such structural-functional relationships will facilitate the development of second-generation products displaying a PTM profile engineered to optimize therapeutic usefulness.
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