| 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. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 17 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Bachelor | 4 | 24% |
| Researcher | 3 | 18% |
| Student > Master | 2 | 12% |
| Student > Ph. D. Student | 2 | 12% |
| Lecturer | 1 | 6% |
| Other | 2 | 12% |
| Unknown | 3 | 18% |
| Readers by discipline | Count | As % |
|---|---|---|
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| Agricultural and Biological Sciences | 4 | 24% |
| Chemistry | 3 | 18% |
| Chemical Engineering | 1 | 6% |
| Environmental Science | 1 | 6% |
| Other | 0 | 0% |
| Unknown | 3 | 18% |