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Evidence for CCl/CBr⋅⋅⋅π Interactions as an Important Contribution to Protein–Ligand Binding Affinity
Abstract
Attractive chlorine: Noncovalent interactions between chlorine or bromine atoms and aromatic rings in proteins open up a new method for the manipulation of molecular recognition. Substitution at distinct positions of two factor Xa inhibitors improves the free energy of binding by interaction with a tyrosine unit. The generality of this motif was underscored by multiple crystal structures as well as high‐level quantum chemical calculations (see picture).magnified image
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Cited by
A Survey of the Role of Noncovalent Sulfur Interactions in Drug Design
Beno, B. R., Yeung, K.-S., Bartberger, M. D., Pennington, L. D., & Meanwell, N. A. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501853m · Cited by 772
Halogen atoms in the modern medicinal chemistry: hints for the drug design
Hernandes, M., Cavalcanti, S. M., Moreira, D. R., de Azevedo Junior, W., & Leite, A. C. (2010) · Current Drug Targets · doi:10.2174/138945010790711996 · Cited by 723
The Bright Future of Unconventional σ/π‐Hole Interactions
Bauzá, A., Mooibroek, T. J., & Frontera, A. (2015) · ChemPhysChem · doi:10.1002/cphc.201500314 · Cited by 710
Halogen bonding (X‐bonding): A biological perspective
Scholfield, M. R., Zanden, C. M. V., Carter, M., & Ho, P. S. (2013) · Protein Science · doi:10.1002/pro.2201 · Cited by 451
A quantum mechanics-based halogen bonding scoring function for protein-ligand interactions.
Yang, Z., Liu, Y., Chen, Z., Xu, Z., Shi, J., Chen, K., & Zhu, W. (2015) · Journal of Molecular Modeling · doi:10.1007/s00894-015-2681-6 · Cited by 23
Metadata
- Authors
- Matter, H., Nazaré, M., Güssregen, S., Will, D. W., Schreuder, H., Bauer, A., Urmann, M., Ritter, K., Wagner, M., & Wehner, V.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2009-03-30
- Volume
- 48
- Issue
- 16
- Pages
- 2911-2916
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2121996197
- Cited by
- 274
- References
- 0
- FWCI
- 13.78
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Evidence for CCl/CBr⋅⋅⋅π Interactions as an Important Contribution to Protein–Ligand Binding Affinity. https://app.cochat.ai/papers/10.1002/anie.200806219
- The paper
- Matter, H., Nazaré, M., Güssregen, S., Will, D. W., Schreuder, H., Bauer, A., Urmann, M., Ritter, K., Wagner, M., & Wehner, V. (2009). Evidence for CCl/CBr⋅⋅⋅π Interactions as an Important Contribution to Protein–Ligand Binding Affinity. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.200806219
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
