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

Maria V. Efremova; Maxim M. Veselov; Alexander V. Barulin; Sergey L. Gribanovsky; Irina M. Le-Deygen; Igor V. Uporov; Elena V. Kudryashova; Marina Sokolsky-Papkov; Alexander G. Majouga; Yuri I. Golovin; Alexander V. Kabanov; Natalia L. Klyachko

doi:10.1021/acsnano.7b06439

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

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

Research output: Contribution to journal › Article › Academic › peer-review

39 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	3190-3199
Number of pages	10
Journal	ACS Nano
Volume	12
Issue number	4
DOIs	https://doi.org/10.1021/acsnano.7b06439
Publication status	Published - 24 Apr 2018
Externally published	Yes

Funding

The authors gratefully acknowledge the financial support of the Russian Science Foundation (grant 14-13-00731), Russian Foundation for Basic Research (grant 17-54-33027 OHKO-a), and Ministry of Education and Science of the Russian Federation in the framework of Increase Competitiveness Program of NUST MISiS No. K2-2016-069. The research was conceived and planned during the Megagrant support (11.G34.31.0004) to establish the Laboratory for Chemical Design of Bionanomaterials in MSU. The authors acknowledge partial support from M.V. Lomonosov Moscow State University Program of Development. The authors gratefully acknowledge the financial support of the Russian Science Foundation (grant 14-13-00731), Russian Foundation for Basic Research (grant 17-54-33027 OHKO_a), and Ministry of Education and Science of the Russian Federation in the framework of Increase Competitiveness Program of NUST “MISiS” No. K2-2016-069. The research was conceived and planned during the Megagrant support (11.G34.31.0004) to establish the “Laboratory for Chemical Design of Bionanomaterials” in MSU. The authors acknowledge partial support from M.V. Lomonosov Moscow State University Program of Development.

Keywords

enzyme
gold-coated magnetite nanoparticles
magnetic nanoparticles
nonheating low-frequency magnetic field
trypsin inhibitor
α-chymotrypsin

Access to Document

10.1021/acsnano.7b06439

Cite this

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. (2018). In Situ Observation of Chymotrypsin Catalytic Activity Change Actuated by Nonheating Low-Frequency Magnetic Field. ACS Nano, 12(4), 3190-3199. https://doi.org/10.1021/acsnano.7b06439

@article{5859adddc8b44fb9816647015b43bb79,

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

abstract = "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.",

keywords = "enzyme, gold-coated magnetite nanoparticles, magnetic nanoparticles, nonheating low-frequency magnetic field, trypsin inhibitor, α-chymotrypsin",

author = "Efremova, \{Maria V.\} and Veselov, \{Maxim M.\} and Barulin, \{Alexander V.\} and Gribanovsky, \{Sergey L.\} and Le-Deygen, \{Irina M.\} and Uporov, \{Igor V.\} and Kudryashova, \{Elena V.\} and Marina Sokolsky-Papkov and Majouga, \{Alexander G.\} and Golovin, \{Yuri I.\} and Kabanov, \{Alexander V.\} and Klyachko, \{Natalia L.\}",

note = "Publisher Copyright: {\textcopyright} 2018 American Chemical Society.",

year = "2018",

month = apr,

day = "24",

doi = "10.1021/acsnano.7b06439",

language = "English",

volume = "12",

pages = "3190--3199",

journal = "ACS Nano",

issn = "1936-0851",

publisher = "American Chemical Society",

number = "4",

}

Efremova, MV, Veselov, MM, Barulin, AV, Gribanovsky, SL, Le-Deygen, IM, Uporov, IV, Kudryashova, EV, Sokolsky-Papkov, M, Majouga, AG, Golovin, YI, Kabanov, AV & Klyachko, NL 2018, 'In Situ Observation of Chymotrypsin Catalytic Activity Change Actuated by Nonheating Low-Frequency Magnetic Field', ACS Nano, vol. 12, no. 4, pp. 3190-3199. https://doi.org/10.1021/acsnano.7b06439

TY - JOUR

T1 - In Situ Observation of Chymotrypsin Catalytic Activity Change Actuated by Nonheating Low-Frequency Magnetic Field

AU - Efremova, Maria V.

AU - Veselov, Maxim M.

AU - Barulin, Alexander V.

AU - Gribanovsky, Sergey L.

AU - Le-Deygen, Irina M.

AU - Uporov, Igor V.

AU - Kudryashova, Elena V.

AU - Sokolsky-Papkov, Marina

AU - Majouga, Alexander G.

AU - Golovin, Yuri I.

AU - Kabanov, Alexander V.

AU - Klyachko, Natalia L.

PY - 2018/4/24

Y1 - 2018/4/24

N2 - 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.

AB - 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.

KW - enzyme

KW - gold-coated magnetite nanoparticles

KW - magnetic nanoparticles

KW - nonheating low-frequency magnetic field

KW - trypsin inhibitor

KW - α-chymotrypsin

UR - https://www.scopus.com/pages/publications/85045896823

U2 - 10.1021/acsnano.7b06439

DO - 10.1021/acsnano.7b06439

M3 - Article

C2 - 29570975

AN - SCOPUS:85045896823

SN - 1936-0851

VL - 12

SP - 3190

EP - 3199

JO - ACS Nano

JF - ACS Nano

IS - 4

ER -

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

Abstract

Funding

Keywords

Access to Document

Other files and links

Fingerprint

Cite this