RESUMO
In this paper, we, for the first time, describe the interaction between the butyrylcholinesterase enzyme and echothiophate, a popular model compound and an analogue of the chemical warfare agents VX and VR, at the atomistic level. Competition between the two echothiophate conformations in the active site was found using molecular modeling techniques. The first one is close to the mode of binding of the substrates of choline series (butyrylcholine and butyrylthiocholine) and is inhibitory, since it is unable to react with the enzyme. The second one is characterized by a significantly worse estimated binding affinity and is reactive. Thus, echothiophate combines the features of two types of inhibitors: competitive and suicidal. This observation will help clarify the kinetic reaction scheme in order to accurately assess the kinetic constants, which is especially important when designing new butyrylcholinesterase variants capable of full-cycle hydrolysis of organophosphorus compounds.
RESUMO
In this research we investigated the response of DNA-modified carbon nanotubes in the presence of thrombin and albumin. We analyzed aptamer-carbon nanotube interactions by Raman spectroscopy and by analyzing resistance after each step of biosensor assembly. We have shown that intensity of G-band decreases due to interconnection of aptamer and carbon nanotube and this also evaluates in decrease of sensor structure resistance. The response of the sensor exposed to thrombin and albumin differs essentially from each other. This fact serves as the prerequisite for the development of a highly selective biosensor. Results of this investigation can be used in creation of new generation of personal health monitoring systems.
