我室吴川六教授在J. Am. Chem. Soc.上发表题为'Orthogonal Cysteine-Penicillamine Disulfide Pairing for Directing the Oxidative Folding of Peptides'的研究论文。

相关链接：http://pubs.acs.org/doi/abs/10.1021/jacs.5b10779

Abstract
Precise disulfide pairing in synthetic peptides is usually achieved using orthogonal protecting group strategies or relies on primary sequence manipulation. Orthogonal disulfide pairing technology should be promising for directing the rational folding of multicyclic peptides from the fully reduced peptides. Here, we report an important discovery on the orthogonality between hetero-disulfide pairing of cysteine (Cys) and penicillamine (Pen) and formation of Cys-Cys/Pen-Pen homo-disulfides. The orthogonal Cys-Pen disulfide pairing can be exploited for highly selective production of certain (multi)cyclic structures (or even a sole structure without isomers) through direct oxidation in air or thiol-disulfide exchanges in redox media. This strategy makes rational folding of multicyclic peptides without protecting groups, sequence manipulation, and complex synthetic reactions a reality, thus providing invaluable assets to peptide communities and would greatly benefit the development of multicyclic peptide therapeutics and ligands.