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Role of Engineered Proteins as Therapeutic Formulations
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Khushboo Gulati, Krishna Mohan Poluri
In the current era of modern medicines, protein therapeutics has gained an upper hand as a result of advancements in protein engineering techniques. The global protein therapeutics market was $140,109 million in 2016 and is expected to reach to $217,591 million in 2023 at an annual growth rate (AGR) of 10.9% from 2016 to 2023 (Sumant and Shaikh, 2017). Novel protein drugs are being discovered, and efforts are in progress to improve their efficacy. Protein therapeutics are being attracted owing to their tendency to treat the previously untreatable diseases such as infertility, chronic renal failure, and dwarfism (Johnson-Leger et al., 2006). Further, high binding selectivity and specificity allow protein therapeutics to act on a particular step in disease pathology in contrast to small molecule drugs that broadly target both harmful and protective immune responses instinctively thereby, causing adverse side effects (Rutgeerts et al., 2006). Protein therapeutics can act in several different modes depending on the origin of the disease. First, if the disease is caused by some undesirable extracellular molecule, then enzyme therapeutics can degrade those molecules specifically. Second, if the disease is due to the deficiency of a particular protein, then protein therapeutics can be given in order to recover the health. Thirdly, if any discrepancy in the signaling pathways or inappropriate immune responses are responsible for a disease, then protein therapeutics can act as inhibitors or activators of the particular cell surface receptor (Wen et al., 2010).
Enzyme Catalysis
Published in Harvey W. Blanch, Douglas S. Clark, Biochemical Engineering, 1997
Harvey W. Blanch, Douglas S. Clark
While enzymes are specific in function, the degree of specificity varies. Some may act on closely related substrates, and are said to exhibit group specificity; others are more exacting in their substrate requirements, and are said to be absolutely specific. The product formed from a particular enzyme and substrate is also unique. Enzymes are able to distinguish between stereochemical forms and only one isomer of a particular substrate may undergo reaction. Surprisingly, enzyme reactions may yield stereospecific products from substrates that possess no asymmetric carbon atoms, as long as one carbon is prochiral. This chirality is a result of at least three-point interaction between substrate and enzyme in the active site of the enzyme. In Figure 1.1, sites 1, 2 and 3 are binding sites on the enzyme. When two of the R groups on the substrate are identical, the molecule has a prochiral center and a chiral center can result from the enzymatic reaction, as the substrate can only "fit" into the active site in one configuration if the site has binding selectivity for three of the R-group substituents. If the substrate has four different R groups, then chirality can be preserved in the reaction as a result of the multipoint attachment.
Pharmacokinetics and Pharmacodynamics of Drugs Delivered to the Lung
Published in Anthony J. Hickey, Sandro R.P. da Rocha, Pharmaceutical Inhalation Aerosol Technology, 2019
Stefanie K. Drescher, Mong-Jen Chen, Jürgen B. Bulitta, Günther Hochhaus
In the second case (Figure 6.10), where pulmonary and systemic effects are mediated through different receptors (e.g., beta-2-adrenergic drugs), a high binding selectivity (high affinity to the β2 receptors, low affinity to the β1 receptor) is important for the pulmonary selectivity; and drug candidates with the highest degree of selectivity are preferred.
Self-assembly as a key player for materials nanoarchitectonics
Published in Science and Technology of Advanced Materials, 2019
Katsuhiko Ariga, Michihiro Nishikawa, Taizo Mori, Jun Takeya, Lok Kumar Shrestha, Jonathan P. Hill
The above-mentioned methodology for molecular recognition, molecular tuning, can be regarded as a novel category of recognition mode (Figure 26) [316–318]. As the basics for the supramolecular chemistry, which was the subject of the 1987 Nobel Prize in Chemistry, the most stable state of host–guest complex determines binding constants and binding selectivity [319–321]. This one-state mechanism is the first generation of molecular recognition mode. Important breakthrough for the molecular recognition was made by Shinkai and co-workers, who demonstrated switching of host structure upon photo-isomerization of an azo-benzene bridge of the host structure [322,323]. This work introduced the concept of switching to create two or more states for the molecular recognition and initiate molecular recognition systems controlled by external stimuli. This switching mechanism is regarded as the second generation of the molecular recognition mode. This switching of molecular systems by external stimuli can be also regarded as the basis for controlling molecular machines, the topic of the 2016 Nobel Prize in Chemistry. Unlike one-state mechanism (the first generation) and switching mechanism (the second generation), molecular tuning mechanism utilizes numerous possibilities of host structures upon continuous conformational changes. Therefore, it could be regarded as the third generation of molecular recognition. This new mode is based on the most fundamental nature of organic molecules, conformational flexibility.