Activating Effect of 3‐Benzylidene Oxindoles on AMPK: From Computer Simulation to High‐Content Screening

AMP‐activated protein kinase (AMPK) is currently the subject of intensive study and active discussions. AMPK performs its functions both at the cellular level, providing the switch between energy‐consuming and energy‐producing processes, and at the whole body level, particularly, regulating certain...

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Vydané v:ChemMedChem Ročník 15; číslo 24; s. 2521 - 2529
Hlavní autori: Novikova, Daria S., Grigoreva, Tatyana A., Ivanov, Gleb S., Melino, Gerry, Barlev, Nickolai A., Tribulovich, Vyacheslav G.
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: WEINHEIM Wiley 15.12.2020
Wiley Subscription Services, Inc
Predmet:
AMP
AMPK
Binding sites
Chemistry, Medicinal
Computer simulation
Domains
Fluorescence resonance energy transfer
FRET
high-content screening
Kinases
Life Sciences & Biomedicine
molecular modeling
Pharmacology & Pharmacy
Protein kinase
Science & Technology
Screening
structure-activity relationships
TARGET
PROTEIN-KINASE
PREVENTION
high-content screening
AUTOINHIBITION
structure-activity relationships
METABOLISM
molecular modeling
STRUCTURAL BASIS
AMPK
FRET
INHIBITORS
DERIVATIVES
BINDING
ISSN:1860-7179, 1860-7187, 1860-7187
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Abstract AMP‐activated protein kinase (AMPK) is currently the subject of intensive study and active discussions. AMPK performs its functions both at the cellular level, providing the switch between energy‐consuming and energy‐producing processes, and at the whole body level, particularly, regulating certain aspects of higher nervous activity and behavior. Control of such a ‘main switch’ compensates dysfunctions and associated diseases. In the present paper, we studied the binding of 3‐benzylidene oxindoles to the kinase domain of the AMPK α‐subunit, which is thought to prevent its interaction with the autoinhibitory domain and thus result in the AMPK activation. For this purpose, we developed the cellular test system based on the AMPKAR plasmid, which implements the FRET effect, synthesized a number of 3‐benzylidene oxindole compounds and simulated their binding to various sites of the kinase domain. The most probable binding site for the studied compounds was established by the correlation of calculated and experimental data. The obtained results allow to analyze various classes of AMPK activators using virtual and high‐content screening. Content counts: The binding site of 3‐benzylidene oxindoles within the kinase domain of AMP‐activated protein kinase (AMPK) was established by correlating calculated and experimental activities. Such binding to the kinase domain leads to AMPK activation. A cell model based on the FRET effect was used under HCS conditions to evaluate target activity.
AbstractList AMP‐activated protein kinase (AMPK) is currently the subject of intensive study and active discussions. AMPK performs its functions both at the cellular level, providing the switch between energy‐consuming and energy‐producing processes, and at the whole body level, particularly, regulating certain aspects of higher nervous activity and behavior. Control of such a ‘main switch’ compensates dysfunctions and associated diseases. In the present paper, we studied the binding of 3‐benzylidene oxindoles to the kinase domain of the AMPK α‐subunit, which is thought to prevent its interaction with the autoinhibitory domain and thus result in the AMPK activation. For this purpose, we developed the cellular test system based on the AMPKAR plasmid, which implements the FRET effect, synthesized a number of 3‐benzylidene oxindole compounds and simulated their binding to various sites of the kinase domain. The most probable binding site for the studied compounds was established by the correlation of calculated and experimental data. The obtained results allow to analyze various classes of AMPK activators using virtual and high‐content screening. Content counts: The binding site of 3‐benzylidene oxindoles within the kinase domain of AMP‐activated protein kinase (AMPK) was established by correlating calculated and experimental activities. Such binding to the kinase domain leads to AMPK activation. A cell model based on the FRET effect was used under HCS conditions to evaluate target activity.
AMP-activated protein kinase (AMPK) is currently the subject of intensive study and active discussions. AMPK performs its functions both at the cellular level, providing the switch between energy-consuming and energy-producing processes, and at the whole body level, particularly, regulating certain aspects of higher nervous activity and behavior. Control of such a 'main switch' compensates dysfunctions and associated diseases. In the present paper, we studied the binding of 3-benzylidene oxindoles to the kinase domain of the AMPK alpha-subunit, which is thought to prevent its interaction with the autoinhibitory domain and thus result in the AMPK activation. For this purpose, we developed the cellular test system based on the AMPKAR plasmid, which implements the FRET effect, synthesized a number of 3-benzylidene oxindole compounds and simulated their binding to various sites of the kinase domain. The most probable binding site for the studied compounds was established by the correlation of calculated and experimental data. The obtained results allow to analyze various classes of AMPK activators using virtual and high-content screening.
AMP-activated protein kinase (AMPK) is currently the subject of intensive study and active discussions. AMPK performs its functions both at the cellular level, providing the switch between energy-consuming and energy-producing processes, and at the whole body level, particularly, regulating certain aspects of higher nervous activity and behavior. Control of such a 'main switch' compensates dysfunctions and associated diseases. In the present paper, we studied the binding of 3-benzylidene oxindoles to the kinase domain of the AMPK α-subunit, which is thought to prevent its interaction with the autoinhibitory domain and thus result in the AMPK activation. For this purpose, we developed the cellular test system based on the AMPKAR plasmid, which implements the FRET effect, synthesized a number of 3-benzylidene oxindole compounds and simulated their binding to various sites of the kinase domain. The most probable binding site for the studied compounds was established by the correlation of calculated and experimental data. The obtained results allow to analyze various classes of AMPK activators using virtual and high-content screening.
AMP-activated protein kinase (AMPK) is currently the subject of intensive study and active discussions. AMPK performs its functions both at the cellular level, providing the switch between energy-consuming and energy-producing processes, and at the whole body level, particularly, regulating certain aspects of higher nervous activity and behavior. Control of such a 'main switch' compensates dysfunctions and associated diseases. In the present paper, we studied the binding of 3-benzylidene oxindoles to the kinase domain of the AMPK α-subunit, which is thought to prevent its interaction with the autoinhibitory domain and thus result in the AMPK activation. For this purpose, we developed the cellular test system based on the AMPKAR plasmid, which implements the FRET effect, synthesized a number of 3-benzylidene oxindole compounds and simulated their binding to various sites of the kinase domain. The most probable binding site for the studied compounds was established by the correlation of calculated and experimental data. The obtained results allow to analyze various classes of AMPK activators using virtual and high-content screening.AMP-activated protein kinase (AMPK) is currently the subject of intensive study and active discussions. AMPK performs its functions both at the cellular level, providing the switch between energy-consuming and energy-producing processes, and at the whole body level, particularly, regulating certain aspects of higher nervous activity and behavior. Control of such a 'main switch' compensates dysfunctions and associated diseases. In the present paper, we studied the binding of 3-benzylidene oxindoles to the kinase domain of the AMPK α-subunit, which is thought to prevent its interaction with the autoinhibitory domain and thus result in the AMPK activation. For this purpose, we developed the cellular test system based on the AMPKAR plasmid, which implements the FRET effect, synthesized a number of 3-benzylidene oxindole compounds and simulated their binding to various sites of the kinase domain. The most probable binding site for the studied compounds was established by the correlation of calculated and experimental data. The obtained results allow to analyze various classes of AMPK activators using virtual and high-content screening.
Author Melino, Gerry
Ivanov, Gleb S.
Grigoreva, Tatyana A.
Novikova, Daria S.
Tribulovich, Vyacheslav G.
Barlev, Nickolai A.
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  orcidid: 0000-0001-7723-4962
  surname: Tribulovich
  fullname: Tribulovich, Vyacheslav G.
  organization: Saint Petersburg State Institute of Technology (Technical University)
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Issue 24
Keywords TARGET
PROTEIN-KINASE
PREVENTION
high-content screening
AUTOINHIBITION
structure-activity relationships
METABOLISM
molecular modeling
STRUCTURAL BASIS
AMPK
FRET
INHIBITORS
DERIVATIVES
BINDING
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Snippet AMP‐activated protein kinase (AMPK) is currently the subject of intensive study and active discussions. AMPK performs its functions both at the cellular level,...
AMP-activated protein kinase (AMPK) is currently the subject of intensive study and active discussions. AMPK performs its functions both at the cellular level,...
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SubjectTerms AMP
AMPK
Binding sites
Chemistry, Medicinal
Computer simulation
Domains
Fluorescence resonance energy transfer
FRET
high-content screening
Kinases
Life Sciences & Biomedicine
molecular modeling
Pharmacology & Pharmacy
Protein kinase
Science & Technology
Screening
structure-activity relationships
Title Activating Effect of 3‐Benzylidene Oxindoles on AMPK: From Computer Simulation to High‐Content Screening
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https://www.ncbi.nlm.nih.gov/pubmed/32762073
https://www.proquest.com/docview/2470188764
https://www.proquest.com/docview/2431815468
Volume 15
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