Optimal Hydrogen Bonding And Drug Design – Term Paper Example

Several researches done have revealed the significances that hydrogen bonding has as far as drug designing is concerned. In a research done to determine the relative contribution of hydrogen bonds and hydrophobic pocket of the c-Src and c-Abl proteins, it was found that hydrogen bonding help alter biding affinity and drug efficacy by stabilizing the ligand sites (Rohan et al 23). Another research to determine the relationship between the CH/n hydrogen bonds in proteins and the drug with proline residue reveals that reveals that the number of CH/n hydrogen bond are important in the recognition of the src homology 3 which is important in signal transduction. Signal transduction is a concept applied by drug designers to determine the effectiveness of a given drug. The research concluded that such protein/ ligand interactions are useful in rational drug design (Jeffrey & Saenger 87).
Furthermore, hydrogen bonding has been implicated to the stabilization of molecular conformation and receptor-ligand recognition and binding. This is due to the fact that a special form of hydrogen bonding called halogen-water-hydrogen bridge, which is formed when, one hydrogen bonding in water mediated hydrogen bond is replaced by halogen bonding, are more thermodynamically stable than other water involved interactions. They concluded that such special hydrogen bonds have latent value in drug design and biological engineering (Zhou, Zou & Tian 174).
Elsewhere, a research was done to estimate the importance of hydrogen-bonding site points. In this study, the researchers wanted to identify hydrogen-bonding site points within the active site of the protein so that they could determine the relationship between the hydrogen boding regions of the incoming ligand, for this case, as drug, and the protein. This was then compared with the control experiment where the hydrogen bonding site points had been removed. The findings from the study concluded that the hydrogen bonding site points plays a significant role in protein-drug interaction and hence this idea can be employed in drug design strategy (Kelly & Mancera 413).
In another study that was done to determine the importance of CH/pi hydrogen bonds in rational drug design, it was found out that those molecules that had more hydrogen bonds were more potent than those with less hydrogen bonds in their ligand segments. The findings from the study concluded that weak hydrogen bonds is useful in rational drug design because can be removed from the body easily (Ozawa & Okazaki 2776).
Works cited
Jeffrey Greg & Saenger William. Hydrogen Bonding in Biological Structures. Springer-Verlag, Berlin, 1991.
Kelly Millard & Mancera Rhode. A new method for estimating the importance of hydrogen- bonding groups in the binding site of a protein. Journal of Computer-Aided Molecular Design [J Comput Aided Mol Des], 17 (7), pp. 401-14. 2003. Print.
Ozawa Tollard & Okazaki Kitaura. Importance of CH/π hydrogen bonds in recognition of the core motif in proline-recognition domains: an ab initio fragment molecular orbital study. Journal of Computational Chemistry [J Comput Chem], 32 (13), pp. 2774-82. 2011. Print.
Rohan Patil, Suranjana Das, Ashley Stanley, Lumbani Yadav, Akulapalli Sudhakar &
Ashok Varma. Optimized Hydrophobic Interactions and Hydrogen Bonding at the Target-Ligand Interface Leads the Pathways of Drug-Designing. 5(8). 2010. Print.
Zhou Pillard, Zou Jang & Tian Fung. Halogen-water-hydrogen bridges in biomolecules. Journal of Structural Biology [J Struct Biol], 169 (2), pp. 172-82. 2010. Print.