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

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-t...

Full description

Saved in:
Bibliographic Details
Published in:Diagnostics (Basel) 2022-04, Vol.12 (4), p.943
Main Authors: Ivanov, Yuri D, Malsagova, Kristina A, Bukharina, Natalia S, Vesnin, Sergey G, Usanov, Sergey A, Tatur, Vadim Yu, Lukyanitsa, Andrei A, Ivanova, Nina D, Konev, Vladimir A, Ziborov, Vadim S
Format: Article
Language:English
Subjects:
brightness temperature
Cancer
CYP102 A1
Cytochrome
Enzymes
Methods
Mutation
Nanoparticles
Proteins
Radiation
Radiometers
radiothermometry
Sensors
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 ( ) 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 M is accompanied by fluctuations of ~0.5-1 °C. At the same time, no 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 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.
ISSN:2075-4418
2075-4418
DOI:10.3390/diagnostics12040943