Synthetic α- and β-Ser-ADP-ribosylated Peptides Reveal α-Ser-ADPr as the Native Epimer | Zendy

Jim Voorneveld | Zendy; J.G.M. Rack | Zendy; Ivan Ahel | Zendy; Herman S. Overkleeft | Zendy; Gijsbert A. van der Marel | Zendy; Dmitri V. Filippov | Zendy

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Synthetic α- and β-Ser-ADP-ribosylated Peptides Reveal α-Ser-ADPr as the Native Epimer

Author(s) -

Jim Voorneveld,

J.G.M. Rack,

Ivan Ahel,

Herman S. Overkleeft,

Gijsbert A. van der Marel,

Dmitri V. Filippov

Publication year - 2018

Publication title -

organic letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.94

H-Index - 239

eISSN - 1523-7060

pISSN - 1523-7052

DOI - 10.1021/acs.orglett.8b01742

Subject(s) - chemistry , peptide , serine , stereochemistry , epimer , anomer , oligopeptide , sequence (biology) , combinatorial chemistry , biochemistry , enzyme

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 evidence is obtained that the α-Ser-ADPr linkage comprises the naturally occurring configuration.

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