Halogen Bonding - A Novel Interaction for Rational Drug Design? Export

@article{citeulike:4306176, abstract = {Although recognized in small molecules for quite some time, the implications of halogen bonding in biomolecular systems are only now coming to light. In this study, several systems of proteins in complex with halogenated ligands have been investigated by using a two-layer QM/MM ONIOM methodology. In all cases, the halogen−oxygen distances are shown to be much less than the van der Waals radius sums. Single-point energy calculations unveil that the interaction becomes comparable in magnitude to classical hydrogen bonding. Furthermore, we found that the strength of the interactions attenuates in the order H ≈ I > Br > Cl. These results agree well with the characteristics discovered within small model halogen-bonded systems. A detailed analysis of the interactions reveals that halogen bonding interactions are responsible for the different conformation of the molecules in the active site. This study would help to establish such interaction as a potential and effective tool in the context of drug design.}, author = {Lu, Yunxiang and Shi, Ting and Wang, Yong and Yang, Huaiyu and Yan, Xiuhua and Luo, Xiaoming and Jiang, Hualiang and Zhu, Weiliang}, citeulike-article-id = {4306176}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/jm9000133}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/jm9000133}, day = {14}, doi = {10.1021/jm9000133}, journal = {Journal of Medicinal Chemistry}, keywords = {halogen-bond}, month = {May}, number = {9}, pages = {2854--2862}, posted-at = {2009-08-25 16:52:45}, priority = {2}, title = {Halogen Bonding - A Novel Interaction for Rational Drug Design?}, url = {http://dx.doi.org/10.1021/jm9000133}, volume = {52}, year = {2009} }

TY - JOUR ID - citeulike:4306176 L3 - citeulike-article-id:4306176 N2 - Although recognized in small molecules for quite some time, the implications of halogen bonding in biomolecular systems are only now coming to light. In this study, several systems of proteins in complex with halogenated ligands have been investigated by using a two-layer QM/MM ONIOM methodology. In all cases, the halogen−oxygen distances are shown to be much less than the van der Waals radius sums. Single-point energy calculations unveil that the interaction becomes comparable in magnitude to classical hydrogen bonding. Furthermore, we found that the strength of the interactions attenuates in the order H ≈ I > Br > Cl. These results agree well with the characteristics discovered within small model halogen-bonded systems. A detailed analysis of the interactions reveals that halogen bonding interactions are responsible for the different conformation of the molecules in the active site. This study would help to establish such interaction as a potential and effective tool in the context of drug design. IS - 9 JF - Journal of Medicinal Chemistry EP - 2862 TI - Halogen Bonding - A Novel Interaction for Rational Drug Design? VL - 52 SP - 2854 KW - halogen-bond AU - Lu, Yunxiang AU - Shi, Ting AU - Wang, Yong AU - Yang, Huaiyu AU - Yan, Xiuhua AU - Luo, Xiaoming AU - Jiang, Hualiang AU - Zhu, Weiliang PY - 2009/05/14/ UR - http://dx.doi.org/10.1021/jm9000133 ER -