ReviewMolecules (Basel, Switzerland)2024
How Do Molecular Tweezers Bind to Proteins? Lessons from X-ray Crystallography.
Review in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Molecular tweezer-peptide conjugates disrupt the protein-protein interaction between survivin and histone H3 essential in mitosis.Beilstein journal of organic chemistry · 2026Article
- Naphthalimide-Buckybowl Tweezer for Selective Recognition of Fullerene CChemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
To understand the biological relevance and mode of action of artificial protein ligands, crystal structures with their protein targets are essential. Here, we describe and investigate all known crystal structures that contain a so-called "molecular tweezer" or one of its derivatives with an attached natural ligand on the respective target protein. The aromatic ring system of these compounds is able to include lysine and arginine side chains, supported by one or two phosphate groups that are attached to the half-moon-shaped molecule. Due to their marked preference for basic amino acids and the fully reversible binding mode, molecular tweezers are able to counteract pathologic protein aggregation and are currently being developed as disease-modifying therapies against neurodegenerative diseases such as Alzheimer's and Parkinson's disease. We analyzed the corresponding crystal structures with 14-3-3 proteins in complex with mono- and diphosphate tweezers. Furthermore, we solved crystal structures of two different tweezer variants in complex with the enzyme Δ
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