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Post-translational modifications in the context of therapeutic proteins.

Authors
Type
Published Article
Journal
Nature biotechnology
Publication Date
Volume
24
Issue
10
Pages
1241–1252
Identifiers
PMID: 17033665
Source
Medline
License
Unknown

Abstract

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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