Radiothermometric Study of the Effect of Amino Acid Mutation on the Characteristics of the Enzymatic System.

Autor: Ivanov YD; Laboratory of Nanobiotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10 Build. 8, 119121 Moscow, Russia.; Laboratory of Shock Wave Impacts, Joint Institute for High Temperatures of Russian Academy of Sciences, Izhorskaya St. 13 Build. 2, 125412 Moscow, Russia., Malsagova KA; Laboratory of Nanobiotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10 Build. 8, 119121 Moscow, Russia., Bukharina NS; Laboratory of Nanobiotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10 Build. 8, 119121 Moscow, Russia., Vesnin SG; RES Ltd., Bolshaya Pochtovaya St. 22, 105082 Moscow, Russia., Usanov SA; Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Academician V.F. Kuprevich 5 Build. 2, 220141 Minsk, Belarus., Tatur VY; Foundation of Perspective Technologies and Novations, Shipilovskaya St. 64, 115682 Moscow, Russia., Lukyanitsa AA; Foundation of Perspective Technologies and Novations, Shipilovskaya St. 64, 115682 Moscow, Russia., Ivanova ND; Skryabin Moscow State Academy of Veterinary Medicine and Biotechnology, Academician Skryabin St. 23, 109472 Moscow, Russia., Konev VA; Department of Infectious Diseases in Children, Faculty of Pediatrics, Pirogov Russian National Research Medical University, Ostrovityanov St. 1, 117997 Moscow, Russia., Ziborov VS; Laboratory of Nanobiotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10 Build. 8, 119121 Moscow, Russia.; Laboratory of Shock Wave Impacts, Joint Institute for High Temperatures of Russian Academy of Sciences, Izhorskaya St. 13 Build. 2, 125412 Moscow, Russia.
Jazyk: angličtina
Zdroj: Diagnostics (Basel, Switzerland) [Diagnostics (Basel)] 2022 Apr 10; Vol. 12 (4). Date of Electronic Publication: 2022 Apr 10.
DOI: 10.3390/diagnostics12040943
Abstrakt: The radiothermometry (RTM) study of a cytochrome-containing system (CYP102 A1) has been conducted in order to demonstrate the applicability of RTM for monitoring changes in the functional activity of an enzyme in case of its point mutation. The study has been performed with the example of the wild-type cytochrome (WT) and its mutant type A264K. CYP102 A1 is a nanoscale protein-enzymatic system of about 10 nm in size. RTM uses a radio detector and can record the corresponding brightness temperature ( T br ) of the nanoscale enzyme solution within the 3.4-4.2 GHz frequency range during enzyme functioning. It was found that the enzymatic reaction during the lauric acid hydroxylation at the wild-type CYP102 A1 (WT) concentration of ~10 -9 M is accompanied by T br fluctuations of ~0.5-1 °C. At the same time, no T br fluctuations are observed for the mutated forms of the enzyme CYP102 A1 (A264K), where one amino acid was replaced. We know that the activity of CYP102 A1 (WT) is ~4 orders of magnitude higher than that of CYP102 A1 (A264K). We therefore concluded that the disappearance of the fluctuation of T br CYP102 A1 (A264K) is associated with a decrease in the activity of the enzyme. This effect can be used to develop new methods for testing the activity of the enzyme that do not require additional labels and expensive equipment, in comparison with calorimetry and spectral methods. The RTM is beginning to find application in the diagnosis of oncological diseases and for the analysis of biochemical processes.
Databáze: MEDLINE
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