|
Process Chemistry
Process chemistry is the arm of pharmaceutical chemistry concerned with the development and optimization of a synthetic scheme and pilot plant procedure to manufacture compounds for the drug development phase. Process chemistry is distinguished from medicinal chemistry, which is the arm of pharmaceutical chemistry tasked with designing and synthesizing molecules on small scale in the early drug discovery phase. Medicinal chemists are largely concerned with synthesizing a large number of compounds as quickly as possible from easily tunable chemical building blocks (usually for SAR studies). In general, the repertoire of reactions utilized in discovery chemistry is somewhat narrow (for example, the Buchwald-Hartwig amination, Suzuki coupling and reductive amination are commonplace reactions). In contrast, process chemists are tasked with identifying a chemical process that is safe, cost and labor efficient, “green,” and reproducible, among other considerations. Oftentimes, in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Medicinal Chemistry
Medicinal or pharmaceutical chemistry is a scientific discipline at the intersection of chemistry and pharmacy involved with designing and developing pharmaceutical drugs. Medicinal chemistry involves the identification, synthesis and development of new chemical entities suitable for therapeutic use. It also includes the study of existing drugs, their biological properties, and their quantitative structure-activity relationships (QSAR). Medicinal chemistry is a highly interdisciplinary science combining organic chemistry with biochemistry, computational chemistry, pharmacology, molecular biology, statistics, and physical chemistry. Compounds used as medicines are most often organic compounds, which are often divided into the broad classes of small organic molecules (e.g., atorvastatin, fluticasone, clopidogrel) and "biologics" (infliximab, erythropoietin, insulin glargine), the latter of which are most often medicinal preparations of proteins (natural and recombinant ant ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Boehringer Ingelheim
C.H. Boehringer Sohn AG & Co. is the parent company of the Boehringer Ingelheim group, which was founded in 1885 by Albert Boehringer in Ingelheim am Rhein, Germany. As of 2018, Boehringer Ingelheim is one of the world's largest pharmaceutical companies, and the largest private one. Headquartered in Ingelheim, it operates globally with 146 affiliates and more than 47,700 employees. Unlike most large pharmaceutical companies which are listed, the company is private and fully owned by the Boehringer, Liebrecht and von Baumbach families. The company's key areas of interest are: respiratory diseases, metabolism, immunology, oncology and diseases of the central nervous system. Boehringer Ingelheim is a full member of the European Federation of Pharmaceutical Industries and Associations (EFPIA). The corporate logo of Boehringer Ingelheim depicts a stylized rendition of the central section of the imperial palace of Charlemagne. History 1885–1999 *1885: Albert Boehringer ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrolases
Hydrolase is a class of enzyme that commonly perform as biochemical catalysts that use water to break a chemical bond, which typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases. Esterases cleave ester bonds in lipids and phosphatases cleave phosphate groups off molecules. An example of crucial esterase is acetylcholine esterase, which assists in transforming the neuron impulse into the acetate group after the hydrolase breaks the acetylcholine into choline and acetic acid. Acetic acid is an important metabolite in the body and a critical intermediate for other reactions such as glycolysis. Lipases hydrolyze glycerides. Glycosidases cleave sugar molecules off carbohydrates and peptidases hydrolyze peptide bonds. Nucleosidases hydrolyze the bonds of nucleotides. Hydrolase enzymes are important for the body because they have d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transaminase
Transaminases or aminotransferases are enzymes that catalyze a transamination reaction between an amino acid and an α-keto acid. They are important in the synthesis of amino acids, which form proteins. Function and mechanism An amino acid contains an amine (NH2) group. A keto acid contains a keto (=O) group. In transamination, the NH2 group on one molecule is exchanged with the =O group on the other molecule. The amino acid becomes a keto acid, and the keto acid becomes an amino acid. Most transaminases are protein enzymes. However, some transamination activities of the ribosome have been found to be catalyzed by ribozymes (RNA enzymes). Examples being the hammerhead ribozyme, the VS ribozyme and the hairpin ribozyme. Transaminases require the coenzyme pyridoxal phosphate, which is converted into pyridoxamine in the first half-reaction, when an amino acid is converted into a keto acid. Enzyme-bound pyridoxamine in turn reacts with pyruvate, oxaloacetate, or alpha-ketoglut ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aldo-keto Reductase
The aldo-keto reductase family is a family of proteins that are subdivided into 16 categories; these include a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, prostaglandin F synthase, xylose reductase, rho crystallin, and many others. Structure All possess a similar structure, with a beta-alpha-beta fold characteristic of nucleotide binding proteins. The fold comprises a parallel beta-8/alpha-8-barrel, which contains a novel NADP-binding motif. The binding site is located in a large, deep, elliptical pocket in the C-terminal end of the beta sheet, the substrate being bound in an extended conformation. The hydrophobic nature of the pocket favours aromatic and apolar substrates over highly polar ones. Binding of the NADPH coenzyme causes a massive conformational change, reorienting a loop, effectively locking the coenzyme in place. This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases. Examples Som ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biocatalysis
Biocatalysis refers to the use of living (biological) systems or their parts to speed up (catalyze) chemical reactions. In biocatalytic processes, natural catalysts, such as enzymes, perform chemical transformations on organic compounds. Both enzymes that have been more or less isolated and enzymes still residing inside living cells are employed for this task. Modern biotechnology, specifically directed evolution, has made the production of modified or non-natural enzymes possible. This has enabled the development of enzymes that can catalyze novel small molecule transformations that may be difficult or impossible using classical synthetic organic chemistry. Utilizing natural or modified enzymes to perform organic synthesis is termed chemoenzymatic synthesis; the reactions performed by the enzyme are classified as chemoenzymatic reactions. History Biocatalysis underpins some of the oldest chemical transformations known to humans, for brewing predates recorded history. The olde ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nucleophilic Aromatic Substitution
A nucleophilic aromatic substitution is a substitution reaction in organic chemistry in which the nucleophile displaces a good leaving group, such as a halide, on an aromatic ring. Aromatic rings are usually nucleophilic, but some aromatic compounds do undergo nucleophilic substitution. Just as normally nucleophilic alkenes can be made to undergo conjugate substitution if they carry electron-withdrawing substituents, so normally nucleophilic aromatic rings also become electrophilic if they have the right substituents.This reaction differs from a common SN2 reaction, because it happens at a trigonal carbon atom (sp2 hybridization). The mechanism of SN2 reaction does not occur due to steric hindrance of the benzene ring. In order to attack the C atom, the nucleophile must approach in line with the C-LG (leaving group) bond from the back, where the benzene ring lies. It follows the general rule for which SN2 reactions occur only at a tetrahedral carbon atom. The SN1 mechanism is p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tert-butyloxycarbonyl Protecting Group
The ''tert''-butyloxycarbonyl protecting group or ''tert''-butoxycarbonyl protecting group (BOC group) is a protecting group used in organic synthesis. The BOC group can be added to the amine under aqueous conditions using di-''tert''-butyl dicarbonate in the presence of a base such as sodium carbonate: Protection of the amine can also be accomplished in acetonitrile solution using 4-dimethylaminopyridine (DMAP) as the base. Removal of the BOC in amino acids can be accomplished with strong acids such as trifluoroacetic acid in dichloromethane, or with HCl in methanol. A complication may be the tendency of the ''t''-butyl cation intermediate to alkylate other nucleophiles; scavengers such as anisole or thioanisole may be used. Selective cleavage of the ''N''-Boc group in the presence of other protecting groups is possible when using AlCl3. Sequential treatment with trimethylsilyl iodide then methanol can also be used for Boc deprotection, especially where other deprotecti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Quinoline
Quinoline is a heterocyclic aromatic organic compound with the chemical formula C9H7N. It is a colorless hygroscopic liquid with a strong odor. Aged samples, especially if exposed to light, become yellow and later brown. Quinoline is only slightly soluble in cold water but dissolves readily in hot water and most organic solvents. Quinoline itself has few applications, but many of its derivatives are useful in diverse applications. A prominent example is quinine, an alkaloid found in plants. Over 200 biologically active quinoline and quinazoline alkaloids are identified. 4-Hydroxy-2-alkylquinolines (HAQs) are involved in antibiotic resistance. Occurrence and isolation Quinoline was first extracted from coal tar in 1834 by German chemist Friedlieb Ferdinand Runge; he called quinoline ''leukol'' ("white oil" in Greek). Coal tar remains the principal source of commercial quinoline. In 1842, French chemist Charles Gerhardt obtained a compound by dry distilling quinine, stry ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SN2 Reaction
The SN2 reaction is a type of reaction mechanism that is common in organic chemistry. In this mechanism, one bond is broken and one bond is formed in a concerted way, i.e., in one step. The name SN2 refers to the Hughes-Ingold symbol of the mechanism: "SN" indicates that the reaction is a nucleophilic substitution, and "2" that it proceeds via a bi-molecular mechanism, which means both the reacting species are involved in the rate-determining step. The other major type of nucleophilic substitution is the SN1, but many other more specialized mechanisms describe substitution reactions. The SN2 reaction can be considered as an analogue of the associative substitution in the field of inorganic chemistry. Reaction mechanism The reaction most often occurs at an aliphatic sp3 carbon center with an electronegative, stable leaving group attached to it (often denoted X), which is frequently a halide atom. The breaking of the C–X bond and the formation of the new bond (often deno ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
