Daniel Tietze

University of Gothenburg

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Alesia A. Tietze

University of Gothenburg

Gerd Buntkowsky

Technical University of Darmstadt

Diana Imhof

University of Bonn

Torsten Gutmann

Technical University of Darmstadt

Harald Kolmar

Technical University of Darmstadt

Olga Avrutina

Technical University of Darmstadt

Oliver Ohlenschläger

Leibniz Institute on Aging - Fritz Lipmann Institute (FLI)

Matthias Görlach

Leibniz Institute on Aging - Fritz Lipmann Institute (FLI)

Evi Kostenis

University of Bonn

Pascal Heimer

University of Bonn

Cooperative Institutions

University of Bonn

Technical University of Darmstadt

Friedrich Schiller University Jena

University of Gothenburg

Centre National de la Recherche Scientifique

Freie Universität Berlin

Schiller International University

Iowa State University

University of Würzburg

Chalmers University of Technology

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ChemInform Abstract: NMR Crystallography of Amides, Peptides and Protein‐Ligand Complexes

ChemInform (2013)

Sven Macholl Daniel Tietze Gerd Buntkowsky

Abstract Review: 66 refs.

10.1002/chin.201401279

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Citations (0)

Photosensitized oxidation of citronellol in microreactors

Journal of Photochemistry and Photobiology A Chemistry (2006)

Susann Meyer Daniel Tietze Sven Rau Bernhard Schäfer Günter Kreisel

Citronellol

Microreactor

10.1016/j.jphotochem.2006.08.014

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Citations (96)

Native Chemical Ligation of Highly Hydrophobic Peptides in Ionic Liquid-Containing Media

The Journal of Organic Chemistry (2021)

Andreas C. Baumruck Jie Yang Gerke-Fabian Thomas Luisa I. Beyer Daniel Tietze

The chemical synthesis of a highly hydrophobic membrane-associated peptide by native chemical ligation (NCL) in an ionic liquid (IL) [C2mim][OAc]/buffer mixture was achieved by employing peptide concentrations up to 11 mM. NCL was studied at different pH and water content and compared to several "gold-standard" ligation protocols. The optimized reaction protocol for the NCL in IL required the addition of 40% water and pH adjustment to 7.0–7.5, resulting in ligation yields of up to 80–95% within 1 to 4 h. This new ligation protocol is generally applicable and outperforms current "gold-standard" NCL methods.

Native chemical ligation

Chemical Ligation

10.1021/acs.joc.0c02498

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Citations (6)

Fluorescence Labeling of Peptides: Finding the Optimal Protocol for Coupling Various Dyes to ATCUN-like Structures

ACS Organic & Inorganic Au (2024)

Jordi C. J. Hintzen Shitanshu Devrani Andrew J. Carrod M. Bahadir Bayik Daniel Tietze

Labeling of peptides and proteins with fluorescent dyes is a key step in functionalizing these structures for a wide array of biological assays. However, coupling strategies of such dyes have not been optimized for the most common compounds, while this step is typically the most precious and costly of the whole synthesis. We searched for the best conditions for attachment of the most widely used fluorescent dyes such as 6-carboxyfluorescein, Rhodamine B, and BODIPY-FL to peptides, where amino terminal Cu(II) and Ni(II) binding site (ATCUN) peptides were used as a model system. Surprisingly, conventional methods of dye attachment proved to not be satisfactory and yielded poor efficiency results. We have discovered that when labeling primary amines on peptides, the uncommon synthesis of activated pentafluorophenol (PFP) esters is the most efficient strategy, expedited by microwave irradiation. Coupling to secondary amines is achieved most efficiently through conventional coupling reagents such as HATU and PyBOP. Furthermore, we have employed our fluorescently labeled ATCUN peptides in studies for Cu(II) and Ni(II) sensing, showing that changing the fluorophore does not significantly affect the fluorescence quenching process and discovering the optimal linker length between the ATCUN core and the dye, expanding the repertoire of fluorophores that can be used in this application.

Rhodamine

Linker

BODIPY

10.1021/acsorginorgau.4c00030

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Citations (0)

Structural and Dynamical Basis of G Protein Inhibition by YM-254890 and FR900359: An Inhibitor in Action

Journal of Chemical Information and Modeling (2019)

Daniel Tietze Desirée Kaufmann Alesia A. Tietze Andreas M. Voll Raphael Reher

Specific inhibition of G proteins holds a great pharmacological promise to, e.g., target oncogenic Gq/11 proteins and can be achieved by the two natural products FR900359 (FR) and YM-254890 (YM). Unfortunately, recent rational-design-based approaches to address G proteins other than Gq/11/14 subtypes were not successful mainly due to the conformational complexity of these new modalities-like compounds. Here, we report the water-derived NMR structure of YM, which strongly differs from the conformation of Gq-bound YM as found in the crystal structure. Reanalysis of the crystal structure suggests that the water-derived NMR structure of YM also represents a valid solution of the electron density. Extensive molecular dynamic simulations unveiled much higher binding affinities of the water-derived NMR structure compared to the original YM conformation of pdb 3ah8. Employing a in-silico-designed, fast activating G protein conformation molecular dynamics data ultimately show how the inhibitor impairs the domain motion of the G protein necessary to hinder nucleotide exchange.

Affinities

10.1021/acs.jcim.9b00433

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Citations (30)

Mimicking Nonribosomal Peptides from the Marine Actinomycete Streptomyces sp. H-KF8 Leads to Antimicrobial Peptides

ACS Infectious Diseases (2023)

Luisa I. Beyer Ann-Britt Schäfer Agustina Undabarrena Inger Mattsby‐Baltzer Daniel Tietze

Microorganisms within the marine environment have been shown to be very effective sources of naturally produced antimicrobial peptides (AMPs). Several nonribosomal peptides were identified based on genome mining predictions of

Mode of Action

10.1021/acsinfecdis.3c00206

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Citations (3)

PHIP-label: parahydrogen-induced polarization in propargylglycine-containing synthetic oligopeptides

Chemical Communications (2013)

Marco Körner Grit Sauer Andreas Heil Daichi Nasu Martin Empting

The unsaturated side chain of L-propargylglycine (Pra) was used to study parahydrogen-induced polarization (PHIP) in synthetic oligopeptides. For the first time PHIP-induced NMR signal enhancement was demonstrated using model peptides bearing various functional side chains.

Oligopeptide

Side chain

Induced polarization

10.1039/c3cc43978j

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Citations (30)

Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel

Chemical Science (2018)

Andreas C. Baumruck Daniel Tietze L. K. Steinacker Alesia A. Tietze

In the present study we have developed and optimized a robust strategy for the synthesis of highly hydrophobic peptides, especially membrane proteins, exemplarily using the influenza B M2 proton channel (BM2(1-51)). This strategy is based on the native chemical ligation of two fragments, where the thioester fragment is formed from an oxo-ester peptide, which is synthesized using Fmoc-SPPS, and features an in situ cleavable solubilizing tag (ADO, ADO2 or ADO-Lys5). The nearly quantitative production of the ligation product was followed by an optimized work up protocol, resulting in almost quantitative desulfurization and Acm-group cleavage. Circular dichroism analysis in a POPC lipid membrane revealed that the synthetic BM2(1-51) construct adopts a helical structure similar to that of the previously characterized BM2(1-33).

10.1039/c8sc00004b

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Citations (30)

A Cell-Permeable Inhibitor to Trap Gαq Proteins in the Empty Pocket Conformation

Chemistry & Biology (2014)

Anna-Lena Schmitz Ramona Schrage Evelyn Gaffal Thomas H. Charpentier Johannes Wiest

10.1016/j.chembiol.2014.06.003

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Citations (50)

Ultrasensitive and Selective Copper(II) Detection: Introducing a Bioinspired and Robust Sensor

Chemistry - A European Journal (2020)

Lena K. Müller Ivana Duznovic Daniel Tietze Wadim Weber Mubarak Ali

A nanopore-based CuII -sensing system is reported that allows for an ultrasensitive and selective detection of CuII with the possibility for a broad range of applications, for example in medical diagnostics. A fluorescent ATCUN-like peptide 5/6-FAM-Dap-β-Ala-His is employed to selectively bind CuII ions in the presence of NiII and ZnII and was crafted into ion track-etched nanopores. Upon CuII binding the fluorescence of the peptide sensor is quenched, permitting the detection of CuII in solution. The ion transport characteristics of peptide-modified nanopore are shown to be extremely sensitive and selective towards CuII allowing to sense femtomolar CuII concentrations in human urine mimics. Washing with EDTA fully restores the CuII -binding properties of the sensor, enabling multiple repetitive measurements. The robustness of the system clearly has the potential to be further developed into an easy-to-use, lab-on-chip CuII -sensing device, which will be of great importance for bedside diagnosis and monitor of CuII levels in patients with copper-dysfunctional homeostasis.

Nanopore

Nanosensor

10.1002/chem.202001160

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Citations (25)