Chapter title |
Leveraging Formylglycine-Generating Enzyme for Production of Site-Specifically Modified Bioconjugates
|
---|---|
Chapter number | 1 |
Book title |
Noncanonical Amino Acids
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7574-7_1 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7573-0, 978-1-4939-7574-7
|
Authors |
Robyn M. Barfield, David Rabuka |
Abstract |
Enzymatic modification of proteins can generate uniquely reactive chemical functionality, enabling site-specific reactions on the protein surface. Formylglycine-generating enzyme (FGE) is one enzyme that can be exploited in this fashion. FGE binds its consensus sequence (CXPXR, known as the "aldehyde-tag") and converts the cysteine to a formylglycine (fGly). fGly-containing proteins contain a bioorthogonal aldehyde on their surface that can be modified selectively in the presence of the 20 canonical amino acids. Here, we describe protocols for the generation of a site-specifically modified protein, an antibody-drug conjugate (ADC), using aldehyde-tagging protocols and aldehyde-reactive conjugation chemistry. |
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