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Synfacts 2008(4): 0426-0426  
DOI: 10.1055/s-2008-1042832
Organo- and Biocatalysis
© Georg Thieme Verlag Stuttgart · New York

Biomimetic Diketopiperazine (DKP) and Dipeptide Formation

Contributor(s): Benjamin List, Lars Ratjen
Z.-Z. Huang, L. J. Leman, M. R. Ghadiri*
The Scripps Research Institute, La Jolla, USA
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Publication History

Publication Date:
19 March 2008 (online)

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Significance

The authors report the development of a peptide sequence as a catalyst for amino­acyl transfer of thioesters. The influence of active site juxtaposing amino acid moieties was investigated. Beneficial effects of His and Asp in peptide 1 were observed. With Phe-thioester 2 as substrate, the aminoacyl transfer reaction via dipeptide assembly (see 3) led to the cyclized DKP product 4 in 35% yield (31% of non-cyclized steady-state dipeptide 5). With different substrates the yield of diketopiperazines 4 could be increased up to 85%.