Iron-Catalyzed Biomimetic Dimerization of Tryptophan-Containing Peptides

Biomimetic oxidative dimerization of tryptophan derivatives in aqueous media with oxygen as a bulk oxidant catalyzed by an iron octacarboxy phthalocyanine complex was established. The discovery of the extremely active iron catalyst enables aerobic enzyme-mimetic oxidation to be performed in a flask. This method was applicable to the oxidative dimerization of a wide range of tryptophan derivatives, including various dipeptides and oligopeptides, with remarkable functional-group tolerance without the protection of the amino acid residues. Furthermore, oxidative dimerization of tryptophan derivatives bearing dioxopiperazine units enabled the convergent total synthesis of five natural pyrroloindole compounds and unnatural congeners. The established chemical method provides facile access to a broad range of dimerized peptides with a unique scaffold to link two turn structures, which will serve as a powerful tool to create new small- and medium-sized-molecules as drug candidates.     

A symmetric oxyselenenylation of simple olefins using optically active selenobinaphthyls

Asymmetric trans-addition reactions of simple olefins have been performed by using optically active 2-selenobinaphthyls 1 , 2a–g. Introduction of an amide group at the 2′-position in the binaphthyl skeleton enhances considerably the diastereomeric excess (de) of the asymmetric methoxyselenenylation. In the case of trans-olefins, introduction of another chiral center in the amide group further enhances the de due to double stereodifferentiation between the (R)-binaphthyl skeleton and the chiral amide group introduced at the 2′-position in the binaphthyl skeleton. The use of chiral nucleophiles is also effective to enhance the de for symmetrical cis-olefins.