Semi-Synthesis and Analysis of Chemically Modified Zif268 Zinc-Finger Domains

2012 | journal article. A publication with affiliation to the University of Göttingen.

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​Fehr, Friederike, Andre Nadler, Florian Brodhun, Ivo Feussner, and Ulf Diederichsen. "Semi-Synthesis and Analysis of Chemically Modified Zif268 Zinc-Finger Domains​." ​ChemistryOpen ​1, no. 1 (2012): ​26​-32​. ​https://doi.org/10.1002/open.201100002.

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Authors
Fehr, Friederike; Nadler, Andre; Brodhun, Florian; Feussner, Ivo; Diederichsen, Ulf 
Abstract
Total synthesis of proteins can be challenging despite assembling techniques, such as native chemical ligation (NCL) and expressed protein ligation (EPL). Especially, the combination of recombinant protein expression and chemically addressable solid-phase peptide synthesis (SPPS) is well suited for the redesign of native protein structures. Incorporation of analytical probes and artificial amino acids into full-length natural protein domains, such as the sequence-specific DNA binding zinc-finger motifs, are of interest combining selective DNA recognition and artificial function. The semi-synthesis of the natural 90 amino acid long sequence of the zinc-finger domain of Zif268 is described including various chemically modified constructs. Our approach offers the possibility to exchange any amino acid within the third zinc finger. The realized modifications of the natural sequence include point mutations, attachment of a fluorophore, and the exchange of amino acids at different positions in the zinc finger by artificial amino acids to create additional metal binding sites. The individual constructs were analyzed by circular dichroism (CD) spectroscopy with respect to the integrity of the zinc-finger fold and DNA binding.
Issue Date
2012
Status
published
Publisher
Wiley-v C H Verlag Gmbh
Journal
ChemistryOpen 
ISSN
2191-1363
Sponsor
Deutsche Forschungsgemeinschaft (DFG) [IRTG 1422]

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