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National Repository of Grey Literature 2 records found  Search took 0.00 seconds. 
Microcalorimetry as a method to analyze protein interactions with ligands
 Durčák, Jindřich ; Konvalinka, Jan (advisor) ; Vaněk, Ondřej (referee)
The interactions of proteins with their binding partners occur in every living organisms, in almost every cell process. Therefore the exploration of protein interactions forms significant part of biochemical research. It appears that even more valuable information than the value of equilibrium constants of these interactions is determination of individual energy components - changes in enthalpy and entropy. Thermodynamic analysis by isothermal titration calorimetry (ITC) can determine the changes in entropy and enthalpy caused by formation of complex of binding partners. Microcalorimetry is also an important optimization technique in development of new drugs, for example antiretrovirotics. Despite HIV is a virus known for over 30 years, intensive research has neither brought vaccine nor drug that would permanently cure patients. Already 26 drugs were approved, most of them target viral enzymes reverse transcriptase and protease. Antiretroviral treatment prevents the propagation of HIV and maintains immune system, but long - term use leads to resistance against drugs, which is caused by mutations in the target proteins. One of relatively new targets of therapeutic intervention is capsid core formation of during assembly of new virions. During the assembly many protein - protein interactions take...
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Expression and characterization of recombinant capsid protein from HIV and its mutants: towards inhibition of virus assembly
 Sivá, Monika ; Konvalinka, Jan (advisor) ; Maloy Řezáčová, Pavlína (referee)
Human immunodeficiency virus infection has been a threat to the world for the last thirty years. It causes a condition called acquired immunodeficiency syndrome leading to complete collapse of immune system and death if not treated. There are many anti-HIV drugs that are part of the combined antiretroviral treatment but they only slow down the progress of the infection. Although the success of all the 31 antiviral agents is remarkable, the cure is not efficient enough. The research of potencial new HIV drugs is now focusing on new targets of viral inhibition. The capsid protein is a potential target of virion assembly and maturation inhibitors due to its multimerization features. The N-terminal domains of six capsid proteins create hexamers. These are connected to each other by dimers of the C-terminal domains according to X-ray and NMR studies. There are inhibitors that bind to the C-terminal domain, alter its conformation and weaken the protein-protein interaction of the dimer. Protein calorimetry is a method that could detect and quantify protein-protein interactions and thus capsid protein dimerization and its inhibition. We expressed and purified recombinant wild-type capsid protein and its C-terminal domain that both dimerize in solution and crystals. Their dimerization constant was determined by...
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