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Muhlberg M.,Forschungsinstitut For Molekulare Pharmakologie Fmp | Muhlberg M.,Free University of Berlin | Hoesl M.G.,TU Berlin | Kuehne C.,Charite - Medical University of Berlin | And 4 more authors.
Beilstein Journal of Organic Chemistry | Year: 2015

To add new tools to the repertoire of protein-based multivalent scaffold design, we have developed a novel dual-labeling strategy for proteins that combines residue-specific incorporation of unnatural amino acids with chemical oxidative aldehyde formation at the N-terminus of a protein. Our approach relies on the selective introduction of two different functional moieties in a protein by mutually orthogonal copper-catalyzed azide-alkyne cycloaddition (CuAAC) and oxime ligation. This method was applied to the conjugation of biotin and β-linked galactose residues to yield an enzymatically active thermophilic lipase, which revealed specific binding to Erythrina cristagalli lectin by SPR binding studies. © 2015 Mühlberg et al; licensee Beilstein-Institut.

Sowa S.,Maria Curie Sklodowska University | Muhlberg M.,Free University of Berlin | Muhlberg M.,Forschungsinstitut For Molekulare Pharmakologie Fmp | Pietrusiewicz K.M.,Maria Curie Sklodowska University | And 2 more authors.
Bioorganic and Medicinal Chemistry | Year: 2013

In this paper, we demonstrate the applicability of water-soluble p-dimethylaminoethyl substituted phosphinomethanethiol in acetyl transfer reactions by the traceless Staudinger ligation with unprotected *-azido lysine containing peptides in aqueous buffer systems. Additionally, we present an improved synthesis pathway for the water-soluble phosphinothiol linkers requiring less steps in a comparable overall yield in comparison to previously published protocols. © 2013 Elsevier Ltd. All rights reserved.

Muhlberg M.,Free University of Berlin | Muhlberg M.,Forschungsinstitut For Molekulare Pharmakologie Fmp | Siebertz K.D.,Forschungsinstitut For Molekulare Pharmakologie Fmp | Siebertz K.D.,Humboldt University of Berlin | And 4 more authors.
Chemical Communications | Year: 2014

The thioacid-azide reaction and its chemoselectivity were probed with alkyl azides for a potential application to form amide bonds in aqueous solvents. Our results reveal that under acidic conditions thioamides were formed as major reaction products suggesting a competing mechanism, whereas reactions forming amides predominated at slightly higher pH values. © the Partner Organisations 2014.

Linden A.H.,Forschungsinstitut For Molekulare Pharmakologie Fmp | Franks W.T.,Forschungsinstitut For Molekulare Pharmakologie Fmp | Akbey U.,Forschungsinstitut For Molekulare Pharmakologie Fmp | Lange S.,Forschungsinstitut For Molekulare Pharmakologie Fmp | And 2 more authors.
Journal of Biomolecular NMR | Year: 2011

X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100 K. Protein dynamics are poorly understood below the freezing point of water and down to liquid nitrogen temperatures. Therefore, we investigate the α-spectrin SH3 domain by magic angle spinning (MAS) solid state NMR (ssNMR) at various temperatures while cooling slowly. Cooling down to 95 K, the NMR-signals of SH3 first broaden and at lower temperatures they separate into several peaks. The coalescence temperature differs depending on the individual residue. The broadening is shown to be inhomogeneous by hole-burning experiments. The coalescence behavior of 26 resolved signals (of 62) was compared to water proximity and crystal structure Debye-Waller factors (B-factors). Close proximity to the solvent and large B-factors (i.e. mobility) lead, generally, to a higher coalescence temperature. We interpret a high coalescence temperature as indicative of a large number of magnetically inequivalent populations at cryogenic temperature. © 2011 Springer Science+Business Media B.V.

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