We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Serine-Selective Aerobic Cleavage of Peptides and a Protein Using a Water-Soluble Copper-Organoradical Conjugate.
- Authors
Seki, Yohei; Tanabe, Kana; Sasaki, Daisuke; Sohma, Youhei; Oisaki, Kounosuke; Kanai, Motomu
- Abstract
The site-specific cleavage of peptide bonds is an important chemical modification of biologically relevant macromolecules. The reaction is not only used for routine structural determination of peptides, but is also a potential artificial modulator of protein function. Realizing the substrate scope beyond the conventional chemical or enzymatic cleavage of peptide bonds is, however, a formidable challenge. Here we report a serine-selective peptide-cleavage protocol that proceeds at room temperature and near neutral pH value, through mild aerobic oxidation promoted by a water-soluble copper-organoradical conjugate. The method is applicable to the site-selective cleavage of polypeptides that possess various functional groups. Peptides comprising D-amino acids or sensitive disulfide pairs are competent substrates. The system is extendable to the site-selective cleavage of a native protein, ubiquitin, which comprises more than 70 amino acid residues.
- Subjects
PEPTIDES; PROTEINS; CHEMICAL bonds; CHEMICAL structure; SUPRAMOLECULAR chemistry
- Publication
Angewandte Chemie International Edition, 2014, Vol 53, Issue 25, p6501
- ISSN
1433-7851
- Publication type
Article
- DOI
10.1002/anie.201402618