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Palladium prompted on-demand cysteine chemistry for the synthesis of challenging and uniquely modified proteins

Cysteine side chains are reactive sites of protein synthesis and modification. Here, the authors show that tuning palladium chemoselectivity allows for selective removal of several cysteine protection groups, and use their method to synthesize challenging protein analogues.

Muhammad Jbara
Shay Laps
Ashraf Brik
ResearchOpen Access08 Aug 2018
Nature Communications

Volume: 9, P: 1-11
Histone H3 serine-57 is a CHK1 substrate whose phosphorylation affects DNA repair

Histone post-translational modifications control several fundamental processes on DNA. Here, the authors describe a conserved phosphorylation of histone H3 on the globular core and show that it loosens the nucleosome and regulates DNA repair.

Nikolaos Parisis
Pablo D. Dans
Daniel Fisher
ResearchOpen Access22 Aug 2023
Nature Communications

Volume: 14, P: 1-20
Expanding the chemical toolbox for the synthesis of large and uniquely modified proteins

Chemical protein synthesis can enable the preparation of proteins containing post-translational modifications or unnatural variations such as D-amino acids. Such modified proteins are not easily fabricated by other methods. This Review provides an overview of the current approaches for the chemical synthesis of proteins.

Somasekhar Bondalapati
Muhammad Jbara
Ashraf Brik
Reviews22 Apr 2016
Nature Chemistry

Volume: 8, P: 407-418
Total chemical synthesis of histones and their analogs, assisted by native chemical ligation and palladium complexes

Chemical synthesis of proteins (e.g., histones) allows precise insertion of modified amino acids. This protocol uses palladium chemistry to remove protecting groups and a removable solubilizing tag for the synthesis of lipophilic peptide segments.

Suman Kumar Maity
Muhammad Jbara
Ashraf Brik
Protocols05 Oct 2017
Nature Protocols

Volume: 12, P: 2293-2322

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Palladium prompted on-demand cysteine chemistry for the synthesis of challenging and uniquely modified proteins

Histone H3 serine-57 is a CHK1 substrate whose phosphorylation affects DNA repair

Expanding the chemical toolbox for the synthesis of large and uniquely modified proteins

Total chemical synthesis of histones and their analogs, assisted by native chemical ligation and palladium complexes

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