In Situ Observation of Chymotrypsin Catalytic Activity Change Actuated by Nonheating Low-Frequency Magnetic Field

In Situ Observation of Chymotrypsin Catalytic Activity Change Actuated by Nonheating Low-Frequency Magnetic Field Научная публикация

Журнал

ACS Nano
ISSN: 1936-0851 , E-ISSN: 1936-086X

Вых. Данные

Год: 2018, Том: 12, Номер: 4, Страницы: 3190-3199 Страниц : 10 DOI: 10.1021/acsnano.7b06439

Авторы

Efremova Maria V. ^1,2 , Veselov Maxim M. ¹ , Barulin Alexander V. ¹ , Gribanovsky Sergey L. ³ , Le-Deygen Irina M. ¹ , Uporov Igor V. ¹ , Kudryashova Elena V. ¹ , Sokolsky-Papkov Marina ⁴ , Majouga Alexander G. ^5,1,2 , Golovin Yuri I. ^3,1 , Kabanov Alexander V. ^4,1 , Klyachko Natalia L. ^4,1,2

Организации

1	Laboratory for Chemical Design of Bionanomaterials, Chemistry Department, M.V. Lomonosov Moscow State University, Moscow 119991, Russian Federation
2	National University of Science and Technology MISIS, Moscow 119049, Russian Federation
3	G.R. Derzhavin Tambov State University, Tambov 392036, Russian Federation
4	Center for Nanotechnology in Drug Delivery, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States
5	D. Mendeleev University of Chemical Technology of Russia, Moscow 125047, Russian Federation

Magnetomechanical modulation of biochemical processes is a promising instrument for bioengineering and nanomedicine. This work demonstrates two approaches to control activity of an enzyme, α-chymotrypsin immobilized on the surface of gold-coated magnetite magnetic nanoparticles (GM-MNPs) using a nonheating low-frequency magnetic field (LF MF). The measurement of the enzyme reaction rate was carried out in situ during exposure to the magnetic field. The first approach involves α-chymotrypsin-GM-MNPs conjugates, in which the enzyme undergoes mechanical deformations with the reorientation of the MNPs under LF MF (16–410 Hz frequency, 88 mT flux density). Such mechanical deformations result in conformational changes in α-chymotrypsin structure, as confirmed by infrared spectroscopy and molecular modeling, and lead to a 63% decrease of enzyme initial activity. The second approach involves an α-chymotrypsin–GM-MNPs/trypsin inhibitor–GM-MNPs complex, in which the activity of the enzyme is partially inhibited. In this case the reorientation of MNPs in the field leads to disruption of the enzyme–inhibitor complex and an almost 2-fold increase of enzyme activity. The results further demonstrate the utility of magnetomechanical actuation at the nanoscale for the remote modulation of biochemical reactions.

Efremova M.V. , Veselov M.M. , Barulin A.V. , Gribanovsky S.L. , Le-Deygen I.M. , Uporov I.V. , Kudryashova E.V. , Sokolsky-Papkov M. , Majouga A.G. , Golovin Y.I. , Kabanov A.V. , Klyachko N.L.
In Situ Observation of Chymotrypsin Catalytic Activity Change Actuated by Nonheating Low-Frequency Magnetic Field
ACS Nano. 2018. V.12. N4. P.3190-3199. DOI: 10.1021/acsnano.7b06439 WOS

Web of science:

WOS:000431088200014