Conformationally Unambiguous Spin Label for Exploring the Binding Site Topology of Multivalent Systems

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Multivalent carbohydrate–lectin interactions are a key concept in biological processes mediating, for example, signaling and adhesion. Binding affinities of multivalent ligands often increase by orders of magnitude compared to a monovalent binding situation. Thus, the design of multivalent ligands as potent inhibitors is a highly active field of research, where knowledge about the binding site topology is crucial. Here, we report a general strategy for precise distance measurements between the binding sites of multivalent target proteins using monovalent ligands. We designed and synthesized Monovalent, conformationally Unambiguously Spin-labeled LIgands (MUeSLI). Distances between the binding sites of the multivalent model lectin wheat germ agglutinin in complex with a GlcNAc-derived MUeSLI were determined using pulsed electron paramagnetic resonance spectroscopy. This approach is an efficient method for exploring multivalent systems with monovalent ligands, and it is readily transferable to other target proteins, allowing the targeted design of multivalent ligands without structural information available.

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ISO 690WEICKERT, Sabrina, Torben SEITZ, William K. MYERS, Christiane R. TIMMEL, Malte DRESCHER, Valentin WITTMANN, 2018. Conformationally Unambiguous Spin Label for Exploring the Binding Site Topology of Multivalent Systems. In: The Journal of Physical Chemistry Letters. 2018, 9(20), pp. 6131-6135. eISSN 1948-7185. Available under: doi: 10.1021/acs.jpclett.8b02243
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@article{Weickert2018-10-18Confo-43977,
  year={2018},
  doi={10.1021/acs.jpclett.8b02243},
  title={Conformationally Unambiguous Spin Label for Exploring the Binding Site Topology of Multivalent Systems},
  number={20},
  volume={9},
  journal={The Journal of Physical Chemistry Letters},
  pages={6131--6135},
  author={Weickert, Sabrina and Seitz, Torben and Myers, William K. and Timmel, Christiane R. and Drescher, Malte and Wittmann, Valentin}
}
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    <dcterms:abstract xml:lang="eng">Multivalent carbohydrate–lectin interactions are a key concept in biological processes mediating, for example, signaling and adhesion. Binding affinities of multivalent ligands often increase by orders of magnitude compared to a monovalent binding situation. Thus, the design of multivalent ligands as potent inhibitors is a highly active field of research, where knowledge about the binding site topology is crucial. Here, we report a general strategy for precise distance measurements between the binding sites of multivalent target proteins using monovalent ligands. We designed and synthesized Monovalent, conformationally Unambiguously Spin-labeled LIgands (MUeSLI). Distances between the binding sites of the multivalent model lectin wheat germ agglutinin in complex with a GlcNAc-derived MUeSLI were determined using pulsed electron paramagnetic resonance spectroscopy. This approach is an efficient method for exploring multivalent systems with monovalent ligands, and it is readily transferable to other target proteins, allowing the targeted design of multivalent ligands without structural information available.</dcterms:abstract>
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