Chemical Synthesis of Phosphorylated Insulin-like Growth Factor Binding Protein 2
- 2 April 2021
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 143 (14), 5336-5342
- https://doi.org/10.1021/jacs.1c02280
Abstract
Chemical protein synthesis is a powerful avenue for accessing homogeneously modified proteins. While a significant number of small modified proteins bearing native post-translational modifications and non-natural modifications have been generated to date, access to larger targets has proved challenging. Herein, we describe the use of two ligation manifolds, namely, diselenide–selenoester ligation and native chemical ligation, to assemble a 31.5 kDa phosphorylated insulin-like growth factor binding protein (IGFBP-2) that comprises 290 amino acid residues, a phosphoserine post-translational modification, and nine disulfide bonds.Funding Information
- National Health and Medical Research Council (APP1174941)
- Novo Nordisk Fonden
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