ArticleiScience2024
Interplay of halogen bonding and solvation in protein-ligand binding.
Article in iScience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Article
- Methyllithium and Its Oligomers as Lewis Bases for Hydrogen and Halogen Bonding.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Use of Halogenated Units for the Construction of Artificial Carbohydrate Receptors.Molecules (Basel, Switzerland) · 2026Article
- A novel SaeS-targeting antivirulence antagonist screened against methicillin-resistantFrontiers in cellular and infection microbiology · 2026Article
- From Deep-Sea Natural Product to Optimized Therapeutics: Computational Design of Marizomib Analogs.International journal of molecular sciences · 2025Article
- Multifunctional N-substituted 2-pyridylbenzothiazole derivatives: singlet oxygen generation, protein binding, and photoactivated anticancer and antibacterial activities.RSC advances · 2025Article
- Halogen bonds between ligands and proteins: Can we use them in validation?Protein science : a publication of the Protein Society · 2025Article
- Binding free energy analysis of galectin-3 natural ligands and synthetic inhibitors.Protein science : a publication of the Protein Society · 2025Article
- The nature of halogen bonding: insights from interacting quantum atoms and source function studies.IUCrJ · 2025Article
- End-Point Affinity Estimation of Galectin Ligands by Classical and Semiempirical Quantum Mechanical Potentials.Journal of chemical information and modeling · 2025Article
- Evaluating the antidiabetes and antioxidant activities of halogenated Schiff bases derived from 4-(diethylamino)salicylaldehyde: in vitro antidiabetes, antioxidant and computational investigation.Scientific reports · 2024Article
- Rapid measurement of heteronuclear transverse relaxation rates using non-uniformly sampledMagnetic resonance (Gottingen, Germany) · 2021Article
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Authors and funding
14 authors.
Funding
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Abstract
Halogen bonding is increasingly utilized in efforts to achieve high affinity and selectivity of molecules designed to bind proteins, making it paramount to understand the relationship between structure, dynamics, and thermodynamic driving forces. We present a detailed analysis addressing this problem using a series of protein-ligand complexes involving single halogen substitutions - F, Cl, Br, and I - and nearly identical structures. Isothermal titration calorimetry reveals an increasingly favorable binding enthalpy from F to I that correlates with the halogen size and σ-hole electropositive character, but is partially counteracted by unfavorable entropy, which is constant from F to Cl and Br, but worse for I. Consequently, the binding free energy is roughly equal for Cl, Br, and I. QM and solvation-free-energy calculations reflect an intricate balance between halogen bonding, hydrogen bonds, and solvation. These advances have the potential to aid future drug design initiatives involving halogenated compounds.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.