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Publikationen 2000 - 2004

Proteins with beta-(thienopyrrolyl)alaninies as alternative chromophores and pharmaceutically active amino acids
Zitatschlüssel 017.2001.budisa
Autor Budisa, N. and Alefelder, S. and Bae, J. H. and Golbik, R. and Minks, C. and Huber, R. and Moroder, L.
Seiten 1281-1292
Jahr 2001
DOI 10.1110%2Fps.51601
Journal Prot. Sci.
Jahrgang 10
Nummer 7
Zusammenfassung L-β-(Thieno[3,2-b]pyrrolyl)alanine and L-β-(thieno[2,3-b]pyrrolyl)alanine are mutually isosteric and pharmaceutically active amino acids that mimic tryptophan with the benzene ring in the indole moiety replaced by thiophene. Sulfur as a heteroatom causes physicochemical changes in these tryptophan surrogates that bring about completely new properties not found in the indole moiety. These synthetic amino acids were incorporated into recombinant proteins in response to the Trp UGG codons by fermentation in a Trp-auxotrophic Escherichia coli host strain using the selective pressure incorporation method. Related protein mutants expectedly retain the secondary structure of the native proteins but show significantly changed optical and thermodynamic properties. In this way, new spectral windows, fluorescence, polarity, thermodynamics, or pharmacological properties are inserted into proteins. Such an engineering approach by translational integration of synthetic amino acids with a priori defined properties, as shown in this study, proved to be a novel and useful tool for protein rational design.
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