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A new spin to drug design

MAG-LAB leverages the power of NMR, enhanced by a unique set of protein isotope labeling techniques and decades of expertise in characterizing the driving forces of biomolecular interactions. These technologies are employed to evaluate drug-like molecules with atomic level precision

What we offer:

• Guidance for your hit-to-lead and subsequent lead optimization processes

• Complementation of your X-ray data or circumventing X-ray crystallography when determining small molecule binding sites/poses by combining NMR with computational methods

• Characterizing protein-ligand interactions in atomistic detail where the association happens: in solution

• Making the challenging “undruggable” targets of the proteome accessible

• Understanding the key mechanisms of how molecules interact

Our Mission

We offer in-depth interaction analysis of protein-ligand interfaces using:

NMR Spectroscopy:

  • Atomic resolution

  • Near physiological conditions

  • Bound state dynamics

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Isotope labeling:

  • Highly selective

  • Fully compatible with various expression systems

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We support your medicinal chemistry campaign during:

Hit finding:

  • Analysis of initial hits

  • Selection of Promising Fragments

  • Input for Compound Optimization

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Hit-to-Lead Optimization:

  • Binding mode analysis

  • Input for Functional Group Modification and Fragment Merging

Isotope Labeling

Isoleucine

L01​

L02​

Methionine

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L07​

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L08​

Phenylalanine

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R01

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R03

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R0​2

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R11​

We offer a unique portfolio of stable-isotope labeled small molecules to decorate proteins with deuterium, carbon-13 and/or nitrogen-15 at defined atomic positions

  • fully compatible with routine minimal media E. coli overexpression

  • minimal isotope scrambling

  • high incorporation rates

  • customized isotope labeling patterns available on demand

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Valine and/or Leucine

L03

L05​

L04​

L06​

Alanine

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L09

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L11​

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L10​

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L12​

Tyrosine

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R04​

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R05​

Tryptophan

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R07

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R09

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R0​8

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R10​

Selected research articles:

  • T. Höfurthner, G. Toscano, G. Kontaxis, A, Beier, M. Mayer, L. Geist, DB. McConnell, H. Weinstabl, R. Lichtenecker*, R. Konrat, J. Biomol. NMR 2023

  • G. Platzer, M. Mayer, A. Beier, S. Brueschweiler, J.E. Fuchs, H. Engelhardt, L. Geist, G. Bader, J. Schörghuber, R. Lichtenecker, B. Wolkerstorfer, D. Kessler, D.B. McConnell*, R. Konrat*, Angew. Chem. Int. Ed. 2020, 59, 14861-14868

  • Schörghuber J, Geist L, Platzer G, Feichtinger M, Bisaccia M, Scheibelberger L, Weber F, Lichtenecker RJ* J Biomol NMR 2018, 71, 3, 129-140

  • Schörghuber J, Geist L, Bisaccia M, Weber F, Konrat R, Lichtenecker RJ* J Biomol NMR 2017, 69, 1, 13-22

  • Schörghuber J, Geist L, Platzer G, Konrat R, Lichtenecker RJ* ChemBioChem 2017, 18, 1487–1491

  • Lichtenecker RJ*, Schörghuber J, Bisaccia M Synlett 2015, 26, 2611-2616

  • Schörghuber J, Sara T, Bisaccia M, Schmid W, Konrat R, Lichtenecker RJ* ChemBioChem 2015, 16, 5, 746-751

  • Lichtenecker RJ* Org. Biomol. Chem. 2014, 12, 7551-7560

  • Lichtenecker RJ*, Weinhaeupl K, Schmid W, Konrat R, J. Biomol. NMR 2013 57(4): 327-331

  • Lichtenecker RJ*, Weinhaeupl K, Reuther L, Schoerghuber J, Schmid W, Konrat R J. Biomol. NMR 2013 57(3): 205-209

Histidine

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R06​

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R12​

New in MAG-LAB:

We are constantly expanding our labeling methods to adapt isotope patterns to the needs of our partners and clients, as well as our in-house applications.

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R13

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R14

R15

R16​

R17

NMR-guided drug development

MAG-LAB analyses your protein-ligand interface in atomistic detail using NMR to access information encoded in 1H nuclei

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Assisted by the power of selective precursor labeling and NMR we analyse proteins and ligands in the bound state

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We reveal a detailed picture of

non-covalent interactions as key factors for directed structure optimization

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The four examples below will give you a first glimpse of MAG-LAB's tools and capabilities

#1 Examination of large protein targets

Protein: WDR5

Size: 34KDa

Sample concentration: 50µM

Measurement time: 30min

Selective labeling makes large proteins amenable for NMR characterization and significantly simplifies the spectral appearance of conventional 2D NMR spectra. This makes large protein targets accessible for fragment screening and binding site mapping approaches

Precursors R03, R05 and R10

Precursors L01and L05

MAG-LAB offers expression, purification, and labeling of your protein target

#2 Analysis of interaction surfaces

Selective protein labeling of Brd4-BD1 yields 2D-spectra with high resolution.

Ligand binding results in characteristic chemical shift perturbations, which can be linked to geometrical parameters of energetically favorable CH-π interactions.

Precursors R07 and R18

This work was supported by the Christian Doppler Laboratory of High-Content Structural Biology and Biotechnology and was published in Angew Chem Int Ed  2020, 59, 35, 14861

  • Detection of π-Interactions in solution

  • Applicable at fragment level (low affinities)

  • Suitable for CH3, CH2 and CH donor groups

MAG-LAB offers customized isotope labeling patterns on request

#3 Ligand NMR signals as sensors for interaction

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Valuable information is also contained in ligand chemical shifts. The binding of FKBP12 to the immunophilin GPI1046 is driven by multiple CH-π interactions of the pyrrolidine moiety with aromatic residues on the site of the protein. This interaction results in large chemical shifts (blue and red arrows) which are made visible using our ligand-detected approach.

ChemPhysChem 2024, 25(1), e202300636

#4 Targeting IDPs

Data-driven docking structure of a protein-small molecule complex

3RTau binding to a 3RT specific antibody

Protein-IDP complex structure solved by solution NMR

We offer a wide range of protein/ligand-based NMR experiments that employ tailored protein samples for your drug discovery projects.
Our NMR services include epitope mapping for antigen-antibody interactions, the elucidation of small-molecule binding sites, as well as the characterization of loosely folded or even intrinsically disordered proteins (IDPs)

ChemMedChem 2021, 16 (23), 3576-3587
Acta Neuropathologica 2018, 136, 69-87

Team

Wolfgang Friedl

CEO, Attorney at Law

Robert Konrat

Scientific head and Professor for Structural Biology at the University of Vienna

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Sven Brüschweiler

Researcher (NMR and Structural Biology)

Katharina Siess

Researcher (Molecular Biology and Structural Biology)

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Roman Lichtenecker

Researcher (Head of Organic Chemistry and Scientist at the University of Vienna)

Gerald Platzer

Researcher (NMR and Structural Biology)

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Matus Hlavac

Researcher (Organic Chemistry)

Sarah Kratzwald

Master Student (Molecular Biology)

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Alisa Wimmer

Master Student (Organic Synthesis)

Contact

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A new spin to drug design

Contact us to learn more about the scope of protein labeling and biomolecular NMR spectroscopy. Become acquainted with the many ways MAG-LAB can endow your project with a new spin

Karl-Farkas-Gasse 22

1030 Vienna, Austria

+43 (0)1 9092208

info@mag-lab.eu

© 2025 by MAG-LAB - All Rights Reserved - Company details

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