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Protein-ligand interactions examples

This experiment provides a nice example of the application of spectroscopy to biochemistry. After presenting the basic theory for the spectroscopic treatment of protein-ligand interactions, a procedure for characterizing the binding of methyl orange to bovine serum albumin is described. [Pg.448]

Several kinetic parameters can be measured on different experimental systems to account for the interaction of a compound with CYPs. For example when studying the metabolic stability of a compound, it could be measured in a recombinant CYP system, in human liver microsomes, in hepatocytes and so on. Each system increases in biological complexity. Although in the recombinant CYP system only the cytochrome under consideration is studied, in the case of the human liver microsomes, there is a pool of enzyme present that includes several CYPs, and finally in the hepatocyte cell system, metabolizing enzymes play an important role in the metabolic compound stability. In addition, transport systems are also present that could involve recirculation or other transport phenomena. The more complex the experimental system, the more difficult it is to extract information on the protein/ligand interaction, albeit it is closer to the in vivo real situation and therefore to the mechanism that is actually working in the body. [Pg.248]

The examples described in this chapter are meant to illustrate the actual application of NMR for the study of protein-ligand interactions in the pharmaceutical industry. In our group, the focus has been mainly on protein observe techniques, as we have been fortunate enough to have a dedicated laboratory for providing both unlabeled and labeled proteins in large quantities. At present, two-dimensional HSQC spectra offer the highest content of information which is not accessible that rapidly by other methods. 2D NMR spectroscopy provides... [Pg.433]

An excellent example of the use of isotope labeling in NMR spectroscopy is in its application to studies of protein structure and protein-ligand interaction. Such studies are of prime importance for drug screening and drug design. Consequently this field of research has been supported by drug companies. [Pg.225]

These presented examples of quantitative descriptions of protein-ligand interactions remain to be a very promising area to address affinity and the selectivity challenge in the future. Those approaches are collectively seen as interesting for a more integrated lead optimization on a simultaneous consideration of numerous balanced descriptors and models for optimization. [Pg.347]

Random polypeptides have traditionally been synthesized by copolymerization of amino acid NCAs. Methods for the synthesis and application of random copolymers have been extensively reviewed (e.g., ref1221), and thus only a single example is given here. A second class of random polypeptides includes organized polymeric assemblies that incorporate bioactive sequences and/or structures. Such polymers have been developed for modulation of protein-ligand interactions/231 protein adsorption to surfaces/241 and cell adhesion/25-281 Several examples for the synthesis of these polymeric assemblies are provided below. [Pg.172]

Table 4.1 Examples of NMR techniques for monitoring protein-ligand interactions. Table 4.1 Examples of NMR techniques for monitoring protein-ligand interactions.
X is known, information about binding location. This can be exploited to direct the screen to a particular site on a protein. This location is typically the active site, but the method can also be used to investigate allosteric sites or protein-protein binding interfaces. In the following, we will describe various practical approaches to covalent capture and provide examples of their application in studying protein-ligand interactions and drug discovery. [Pg.247]

Thus, it is possible to calculate the off-rates of protein-ligand interactions observed for individual amino acid residues of the protein of a verified reaction mechanism. A nice example that shows various cases was recently published for the Apo-Cellular Retinol Binding Protein (97). [Pg.1280]

Weakly polar interactions in proteins and protein-ligand complexes are frequently phenomenologically analyzed and classified in terms of the interacting partners (36). This especially includes interactions with x-sys-tems, such as the NH-T, OH-T, or CH-ir interaction (37, 38), aromatic-aromatic interactions (parallel t-t stacking versus edge-to-face interaction), and the cation-T interaction (39). All of these can mostly be rationalized in terms of electrostatic interactions outlined above that is, they involve interactions between monopoles, dipoles, and quadrupoles (permanent and induced). A more distinct character can be attributed to metal complex-ation, which can play a significant role in individual cases of protein-ligand interactions, as for example in metalloenzymes (2,40, 41). [Pg.286]


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