ReviewMolecules (Basel, Switzerland)2016
Protein-Directed Dynamic Combinatorial Chemistry: A Guide to Protein Ligand and Inhibitor Discovery.
Review in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Recent advances in DNA-encoded dynamic libraries.RSC chemical biology · 2022Review
- Hit-optimization using target-directed dynamic combinatorial chemistry: development of inhibitors of the anti-infective target 1-deoxy-d-xylulose-5-phosphate synthase.Chemical science · 2021Article
- Generative Network Complex for the Automated Generation of Drug-like Molecules.Journal of chemical information and modeling · 2020Article
- Tailored therapeutics based on 1,2,3-1MedChemComm · 2019Review
- Insights into real-time chemical processes in a calcium sensor protein-directed dynamic library.Nature communications · 2019Article
- Generative network complex (GNC) for drug discovery.Communications in information and systems · 2019Article
- Proteintemplat-gesteuerte Fragmentligationen - von der molekularen Erkennung zur Wirkstofffindung.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2017Article
- Protein-Templated Fragment Ligations-From Molecular Recognition to Drug Discovery.Angewandte Chemie (International ed. in English) · 2017Review
- Investigating isoquinoline derivatives for inhibition of inhibitor of apoptosis proteins for ovarian cancer treatment.Drug design, development and therapy · 2017Article
- Foreword: Pacific Fragments.Molecules (Basel, Switzerland) · 2016Article
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2 authors.
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Abstract
Protein-directed dynamic combinatorial chemistry is an emerging technique for efficient discovery of novel chemical structures for binding to a target protein. Typically, this method relies on a library of small molecules that react reversibly with each other to generate a combinatorial library. The components in the combinatorial library are at equilibrium with each other under thermodynamic control. When a protein is added to the equilibrium mixture, and if the protein interacts with any components of the combinatorial library, the position of the equilibrium will shift and those components that interact with the protein will be amplified, which can then be identified by a suitable biophysical technique. Such information is useful as a starting point to guide further organic synthesis of novel protein ligands and enzyme inhibitors. This review uses literature examples to discuss the practicalities of applying this method to inhibitor discovery, in particular, the set-up of the combinatorial library, the reversible reactions that may be employed, and the choice of detection methods to screen protein ligands from a mixture of reversibly forming molecules.
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