Diederichsen, Ulf

[["dc.bibliographiccitation.firstpage","449"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Amino Acids"],["dc.bibliographiccitation.lastpage","456"],["dc.bibliographiccitation.volume","41"],["dc.contributor.author","Sachs, Eike-F."],["dc.contributor.author","Nadler, Andre"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T08:54:54Z"],["dc.date.available","2018-11-07T08:54:54Z"],["dc.date.issued","2011"],["dc.description.abstract","The natural product triostin A is known as an antibiotic based on specific DNA recognition. Structurally, a bicyclic depsipeptide backbone provides a well-defined scaffold preorganizing the recognition motifs for bisintercalation. Replacing the intercalating quinoxaline moieties of triostin A by nucleobases results in a potential major groove binder. The functionalization of this DNA binding triostin A analog with a metal binding ligand system is reported, thereby generating a hybrid molecule with DNA binding and metal coordinating capability. Transition metal ions can be placed in close proximity to dsDNA by means of non-covalent interactions. The synthesis of the nucleobase-modified triostin A analog is described containing a propargylglycine for later attachment of the ligand by click-chemistry. As ligand, two [1,4,7]triazacyclononane rings were bridged by a phenol. Formation of the proposed binuclear zinc complex was confirmed for the ligand and the triostin A analog/ligand construct by high-resolution mass spectrometry. The complex as well as the respective hybrid led to stabilization of dsDNA, thus implying that metal complexation and DNA binding are independent processes."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [Di 542/7-1, IRTG 1422]"],["dc.identifier.doi","10.1007/s00726-010-0764-3"],["dc.identifier.isi","000291034000019"],["dc.identifier.pmid","20967559"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6646"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22780"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.relation.issn","1438-2199"],["dc.relation.issn","0939-4451"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Triostin A derived hybrid for simultaneous DNA binding and metal coordination"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","26"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","ChemistryOpen"],["dc.bibliographiccitation.lastpage","32"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Fehr, Friederike"],["dc.contributor.author","Nadler, Andre"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T09:14:10Z"],["dc.date.available","2018-11-07T09:14:10Z"],["dc.date.issued","2012"],["dc.description.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."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft (DFG) [IRTG 1422]"],["dc.identifier.doi","10.1002/open.201100002"],["dc.identifier.isi","000328606600005"],["dc.identifier.pmid","24551489"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8371"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27345"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","2191-1363"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","Semi-Synthesis and Analysis of Chemically Modified Zif268 Zinc-Finger Domains"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]