| Chapter title |
ADPr-Peptide Synthesis
|
|---|---|
| Chapter number | 24 |
| Book title |
ADP-ribosylation and NAD+ Utilizing Enzymes
|
| Published in |
Methods in molecular biology, August 2018
|
| DOI | 10.1007/978-1-4939-8588-3_24 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-8587-6, 978-1-4939-8588-3
|
| Authors |
Hans A. V. Kistemaker, Jim Voorneveld, Dmitri V. Filippov, Kistemaker, Hans A. V., Voorneveld, Jim, Filippov, Dmitri V. |
| Abstract |
Synthetic mono-ADPr-peptides are useful for structural, biochemical, and proteomics studies. We describe here a protocol for the preparation of mono-ADPr-peptides based on a fairly standard Fmoc-based solid-phase synthesis. Phosphoribosylated precursor building blocks are introduced into the peptide chain on solid-phase and subsequently converted to ADPr-sites by chemical phosphorylation with adenosine phosphoramidite. Suitably protected phosphoribosylated glutamine, asparagine, and citrulline building blocks described in this protocol allow introduction of ADP-Gln, ADPr-Asn, and ADPr-Cit into peptide chains as demonstrated for three peptides. Trifunctional amino acids, for which base-sensitive side-chain protection is available, can be accommodated in the sequences flanking the ADPr-cites. |
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