Czech Institute of Organic Chemistry And Biochemistry

Prague, Czech Republic

Czech Institute of Organic Chemistry And Biochemistry

Prague, Czech Republic
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Czech Institute of Organic Chemistry And Biochemistry | Date: 2017-02-22

The invention provides compounds of formula I, wherein R_(1) and R_(2) have any of the values defined in the specification and salts thereof, as well as compositions comprising such compounds and therapeutic methods that utilize such compounds.


Strisovsky K.,Czech Institute of Organic Chemistry And Biochemistry
The FEBS journal | Year: 2016

Intramembrane proteases (IMPRs) cleave transmembrane proteins inside the lipid bilayer. They regulate a growing number of biological processes, and our knowledge about the evolutionary and functional niches these unusual enzymes have filled is slowly unravelling. Although structures of representative members of four IMPR families have been solved, the mechanism of substrate recognition and cleavage is still poorly understood. Here I offer a view on substrate recognition by IMPRs from the angle of their biological functions. Zooming in on rhomboid proteases I delineate the emerging principles and areas of contention, and argue that by studying the mechanisms, specificity and natural substrate repertoires of IMPRs we can understand the properties for which they have been selected in evolution. © 2015 Federation of European Biochemical Societies.


Schroder D.,Czech Institute of Organic Chemistry And Biochemistry
Angewandte Chemie - International Edition | Year: 2010

Figure Presented Cold methane coupling: Recent experiments with trapped Au2+ clusters reveal a catalytic cycle for the dehydrogenative CC coupling of methane to give ethene at temperatures between 200 and 300 K (see scheme). The key novelty of the work is the explicit exploration of the multicollisional regime, which represents an important step to bridge the pressure gap between model studies and real catalysis. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.


Schroder D.,Czech Institute of Organic Chemistry And Biochemistry
Accounts of Chemical Research | Year: 2012

Mechanistic studies form the basis for a better understanding of chemical processes, helping researchers develop more sustainable reactions by increasing the yields of the desired products, reducing waste production, and lowering the consumption of resources and energy overall. Conventional methods for the investigation of reaction mechanisms in solution include kinetic studies, isotope labeling, trapping of reactive intermediates, and advanced spectroscopic techniques. Within the past decade, electrospray ionization mass spectrometry (ESI-MS) has provided an additional tool for mechanistic studies because researchers can directly probe liquid samples by mass spectrometry under gentle conditions.Specifically, ESI-MS allows researchers to identify the molecular entities present in solution over the course of a chemical transformation. ESI-MS is particularly useful for investigations of organic reactions or metal catalysis that involve ionic intermediates. Accordingly, researchers are increasingly using ESI-MS in mechanistic studies and catalyst development. However, a further understanding of the ESI process and how it can facilitate mechanistic studies has not accompanied this increased use of the technique. Therefore, at least in part the ESI-MS method not only has offered great promise for the elucidation of reaction mechanisms but also became a black box with the occasional risk of misinterpretation.In this Account, we summarize applications of ESI-MS for synthetic and mechanistic research. Recently researchers have established direct linkages between gas-phase data obtained via ESI-MS and processes occurring in solution, and these results reveal qualitative and quantitative correlations between ESI-MS measurements and solution properties. In this context, time dependences, concentration series, and counterion effects can serve as criteria that allow researchers assess if the gas-phase measurements correlate with the situation in the solution. Furthermore, we report developments that bridge the gap between gas-phase and solution-phase studies. We also describe predictions derived from ESI-MS that have been verified with solution-phase chemistry experiments. © 2012 American Chemical Society.


Schroder D.,Czech Institute of Organic Chemistry And Biochemistry
Physical Chemistry Chemical Physics | Year: 2012

Electrospray ionization is suggested as a complementary technique for the investigation of the solution chemistry of metal salts, which allows us to achieve direct insight into the molecular entities present in solution. While the transfer of the metal ions from solution to the gas phase in the course of the electrospray process is associated with significant changes in concentration, pH, and also composition in the case of mixed solvents, systematic studies of concentration series can provide criteria to assess the extent to which the gas-phase data correlate with the situation in solution. While there does not exist a 11 correlation between mass spectrometric measurements and solution properties, very useful qualitative molecular insights can be achieved and quantitative analysis can be made once the specific circumstances of the ionization process are taken into account. © the Owner Societies 2012.


This review summarizes the current status of radical-based transition metal catalyzed reactions in organic chemistry. The underlying features of radical generation from transition metal complexes and radical reactivity in the framework of transition metal catalysis are discussed. The available arsenal to detect radicals in transition metal catalyzed transformations is presented. Available strategies to combine radical intermediates with transition metal catalysis are outlined. In the main part the currently known synthetic methodology of transition metal catalyzed reactions proceeding via radical intermediates is discussed. This part covers catalytic radical reactions involving group 4 to group 7 elements. © 2011 Springer-Verlag Berlin Heidelberg.


This review summarizes the current status of transition metal catalyzed reactions involving radical intermediates in organic chemistry. This part focuses on radical-based methods catalyzed by group 10 and group 11 metal complexes. Reductive and redox-neutral C-C bond formations catalyzed by low-valent metal complexes as well as catalytic oxidative methods are reviewed. Catalytic processes which rely on the combination of two metal complexes are also covered. © 2011 Springer-Verlag Berlin Heidelberg.


This review summarizes the current status of transition metal catalyzed reactions involving radical intermediates in organic chemistry. This part focuses on radical-based methods catalyzed by group 8 and group 9 metal complexes. Reductive and redox-neutral coupling methods catalyzed by low-valent metal complexes as well as catalytic oxidative C-C bond formations are reviewed. © 2011 Springer-Verlag Berlin Heidelberg.


Strisovsky K.,Czech Institute of Organic Chemistry And Biochemistry
FEBS Journal | Year: 2013

Intramembrane proteases cleave membrane proteins in their transmembrane helices to regulate a wide range of biological processes. They catalyse hydrolytic reactions within the hydrophobic environment of lipid membranes where water is normally excluded. How? Do the different classes of intramembrane proteases share any mechanistic principles? In this review these questions will be discussed in view of the crystal structures of prokaryotic members of the three known catalytic types of intramembrane proteases published over the past 7 years. Rhomboids, the intramembrane serine proteases that are the best understood family, will be the initial area of focus, and the principles that have arisen from a number of structural and biochemical studies will be considered. The site-2 metalloprotease and GXGD-type aspartyl protease structures will then be discussed, with parallels drawn and differences highlighted between these enzymes and the rhomboids. Despite the significant advances achieved so far, to obtain a detailed understanding of the mechanism of any intramembrane protease, high-resolution structural information on the substrate-enzyme complex is required. This remains a major challenge for the field. Intramembrane proteases regulate a wide range of biological processes, but their mechanisms are unclear. In this review I discuss the available crystal structures of prokaryotic homologs of all three classes of intramembrane proteases: the rhomboids, the intramembrane aspartyl proteases and metalloproteases, and review our current understanding of their catalytic properties. © 2013 FEBS.


Kasicka V.,Czech Institute of Organic Chemistry And Biochemistry
Electrophoresis | Year: 2014

The review presents a comprehensive survey of recent developments and applications of capillary and microchip electroseparation methods (zone electrophoresis, ITP, IEF, affinity electrophoresis, EKC, and electrochromatography) for analysis, isolation, purification, and physicochemical and biochemical characterization of peptides. Advances in the investigation of electromigration properties of peptides, in the methodology of their analysis, including sample preseparation, preconcentration and derivatization, adsorption suppression and EOF control, as well as in detection of peptides, are presented. New developments in particular CE and CEC modes are reported and several types of their applications to peptide analysis are described: conventional qualitative and quantitative analysis, determination in complex (bio)matrices, monitoring of chemical and enzymatical reactions and physical changes, amino acid, sequence and chiral analysis, and peptide mapping of proteins. Some micropreparative peptide separations are shown and capabilities of CE and CEC techniques to provide relevant physicochemical characteristics of peptides are demonstrated. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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