Journal article
Synthetic α- and β-Ser-ADP-ribosylated peptides reveal α-Ser-ADPr as the native epimer
- Abstract:
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A solid-phase methodology to synthesize oligopeptides, specifically incorporating serine residues linked to ADP-ribose (ADPr), is presented. Through the synthesis of both α- and β-anomers of the phosphoribosylated Fmoc-Ser building block and their usage in our modified solid-phase peptide synthesis protocol, both α- and β-ADPr peptides from a naturally Ser-ADPr containing H2B sequence were obtained. With these, and by digestion studies using the human glycohydrolase, ARH3 (hARH3), compelling ...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 1.5MB)
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- Publisher copy:
- 10.1021/acs.orglett.8b01742
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Authors
Bibliographic Details
- Publisher:
- American Chemical Society Publisher's website
- Journal:
- Organic Letters Journal website
- Volume:
- 20
- Issue:
- 13
- Pages:
- 4140-4143
- Publication date:
- 2018-06-27
- Acceptance date:
- 2018-06-27
- DOI:
- EISSN:
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1523-7052
- ISSN:
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1523-7060
- Source identifiers:
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864373
Item Description
- Pubs id:
-
pubs:864373
- UUID:
-
uuid:8716cfe9-a46b-4022-b2a6-b4510d91d399
- Local pid:
- pubs:864373
- Deposit date:
- 2018-07-04
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2018
- Notes:
-
© 2018 American Chemical Society. This is an open access article published under a Creative Commons Non-Commercial No
Derivative Works (CC-BY-NC-ND) Attribution License, which permits copying and
redistribution of the article, and creation of adaptations, all for non-commercial purposes.
- Licence:
- CC Attribution (CC BY)
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