Home / Publications / The neuropeptide cycloprolylglycine can form a complex with AMPA receptors

The neuropeptide cycloprolylglycine can form a complex with AMPA receptors

Valerij Khalil'bekovich Akparov 1
Valerij Khalil'bekovich Akparov
, 
Vladimir Igorevich Timofeev 2
Vladimir Igorevich Timofeev
, 
Ksenia Nikolaevna Koliasnikova 3
Ksenia Nikolaevna Koliasnikova
10.1016/j.mencom.2022.07.003
Published 2022-07-01
Communication , Volume 32, Issue 4, 436-438
1
Share
Cite this
GOST
 | 
Cite this
GOST Copy
Akparov V. K., Timofeev V. I., Koliasnikova K. N. The neuropeptide cycloprolylglycine can form a complex with AMPA receptors // Mendeleev Communications. 2022. Vol. 32. No. 4. pp. 436-438.
GOST all authors (up to 50) Copy
Akparov V. K., Timofeev V. I., Koliasnikova K. N. The neuropeptide cycloprolylglycine can form a complex with AMPA receptors // Mendeleev Communications. 2022. Vol. 32. No. 4. pp. 436-438.
RIS
 | 
Cite this
RIS Copy
TY - JOUR
DO - 10.1016/j.mencom.2022.07.003
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2022.07.003
TI - The neuropeptide cycloprolylglycine can form a complex with AMPA receptors
T2 - Mendeleev Communications
AU - Akparov, Valerij Khalil'bekovich
AU - Timofeev, Vladimir Igorevich
AU - Koliasnikova, Ksenia Nikolaevna
PY - 2022
DA - 2022/07/01
PB - Mendeleev Communications
SP - 436-438
IS - 4
VL - 32
ER -
BibTex
 | 
Cite this
BibTex (up to 50 authors) Copy
@article{2022_Akparov,
author = {Valerij Khalil'bekovich Akparov and Vladimir Igorevich Timofeev and Ksenia Nikolaevna Koliasnikova},
title = {The neuropeptide cycloprolylglycine can form a complex with AMPA receptors},
journal = {Mendeleev Communications},
year = {2022},
volume = {32},
publisher = {Mendeleev Communications},
month = {Jul},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2022.07.003},
number = {4},
pages = {436--438},
doi = {10.1016/j.mencom.2022.07.003}
}
MLA
Cite this
MLA Copy
Akparov, Valerij Khalil'bekovich, et al. “The neuropeptide cycloprolylglycine can form a complex with AMPA receptors.” Mendeleev Communications, vol. 32, no. 4, Jul. 2022, pp. 436-438. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2022.07.003.

Keywords

allosteric site of AMPA receptor
cycloprolylglycine
endogenous ampakine
MM-GBSA
piracetam

Abstract

The calculations using the MM-GBSA method demonstrated that the neuropeptide cycloprolylglycine, structurally and pharmacologically resembling the classical nootropic piracetam, can bind to the piracetam site of the ligand- binding domain of the GluA3i AMPA receptor subtype with the binding energy higher than that of piracetam. Thus, together with the previous electrophysiological and biochemical data, the computational results confirm that cycloprolylglycine may be an endogenous ampakine.

References

1.
Identification of a novel endogenous memory facilitating cyclic dipeptide cyclo‐prolylglycine in rat brain
Gudasheva T.A., Boyko S.S., Akparov V.K., Ostrovskaya R.U., Skoldinov S.P., Rozantsev G.G., Voronina T.A., Zherdev V.P., Seredenin S.B.
FEBS Letters, 1996
2.
Plasma cyclic glycine proline/ IGF ‐1 ratio predicts clinical outcome and recovery in stroke patients
Fan D., Krishnamurthi R., Harris P., Barber P.A., Guan J.
Annals of Clinical and Translational Neurology, 2019
3.
New endogenous dipeptide cycloprolyl-glycine is similar to piracetam by its mnemotropic selectivity
Gudasheva T.A., Ostrovskaya R.U., Trofimov S.S., Voronina T.A., Skoldinov A.P., Seredenin S.B.
Bulletin of Experimental Biology and Medicine, 1999
4.
10.1016/j.mencom.2022.07.003_b0020
Koliasnikova
Eksp. Klin. Farmakol., 2012
6.
Anxiolytic Activity of Endogenous Nootropic Dipeptide Cycloprolylglycine in Elevated Plus-Maze Test
Gudasheva T.A., Konstantinopol'skii M.A., Ostrovskaya R.U., Seredenin S.B.
Bulletin of Experimental Biology and Medicine, 2001
7.
Neuropeptide cycloprolylglycine is an endogenous positive modulator of AMPA receptors
Gudasheva T.A., Grigoriev V.V., Koliasnikova K.N., Zamoyski V.L., Seredenin S.B.
Doklady Biochemistry and Biophysics, 2016
8.
The Anxiolytic Effect of the Neuropeptide Cycloprolylglycine Is Mediated by AMPA and TrkB Receptors
Gudasheva T.A., Povarnina P.Y., Koliasnikova K.N., Alyaeva A.G., Vorontsova O.N., Seredenin S.B.
Doklady Biochemistry and Biophysics, 2020
9.
Nootropic Drugs Positively Modulate ?-Amino-3-Hydroxy-5-Methyl-4-Isoxazolepropionic Acid-Sensitive Glutamate Receptors in Neuronal Cultures
Copani A., Genazzani A.A., Aleppo G., Casabona G., Canonico P.L., Scapagnini U., Nicoletti F.
Journal of Neurochemistry, 1992
12.
Temnyakova N.S., Vasilenko D.A., Lavrov M.I., Karlov D.S., Grishin Y.K., Zamoyski V.L., Grigoriev V.V., Averina E.B., Palyulin V.A.
Mendeleev Communications, 2021
13.
Temnyakova N.S., Vasilenko D.A., Lavrov M.I., Karlov D.S., Grishin Y.K., Zamoyski V.L., Grigoriev V.V., Averina E.B., Palyulin V.A.
Mendeleev Communications, 2021
14.
Calculating Structures and Free Energies of Complex Molecules:  Combining Molecular Mechanics and Continuum Models
Kollman P.A., Massova I., Reyes C., Kuhn B., Huo S., Chong L., Lee M., Lee T., Duan Y., Wang W., Donini O., Cieplak P., Srinivasan J., Case D.A., Cheatham T.E., et. al.
Accounts of Chemical Research, 2000
15.
Application of a pairwise generalized Born model to proteins and nucleic acids: inclusion of salt effects
Srinivasan J., Trevathan M.W., Beroza P., Case D.A.
Theoretical Chemistry Accounts, 1999
16.
Features and development ofCoot
Emsley P., Lohkamp B., Scott W.G., Cowtan K.
Acta Crystallographica Section D Biological Crystallography, 2010
17.
The Amber biomolecular simulation programs
Case D.A., Cheatham T.E., Darden T., Gohlke H., Luo R., Merz K.M., Onufriev A., Simmerling C., Wang B., Woods R.J.
Journal of Computational Chemistry, 2005
18.
Routine Microsecond Molecular Dynamics Simulations with AMBER on GPUs. 2. Explicit Solvent Particle Mesh Ewald.
Salomon-Ferrer R., Götz A.W., Poole D., Le Grand S., Walker R.C.
Journal of Chemical Theory and Computation, 2013
19.
ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB
Maier J.A., Martinez C., Kasavajhala K., Wickstrom L., Hauser K.E., Simmerling C.
Journal of Chemical Theory and Computation, 2015
20.
10.1016/j.mencom.2022.07.003_b0100
Allen
Computer Simulation of Liquids, 1991
21.
Molecular dynamics with coupling to an external bath
Berendsen H.J., Postma J.P., van Gunsteren W.F., DiNola A., Haak J.R.
Journal of Chemical Physics, 1984
22.
Particle mesh Ewald: AnN⋅log(N) method for Ewald sums in large systems
Darden T., York D., Pedersen L.
Journal of Chemical Physics, 1993
23.
MMPBSA.py: An Efficient Program for End-State Free Energy Calculations
Miller B.R., McGee T.D., Swails J.M., Homeyer N., Gohlke H., Roitberg A.E.
Journal of Chemical Theory and Computation, 2012
24.
Exploring protein native states and large-scale conformational changes with a modified generalized born model
Onufriev A., Bashford D., Case D.A.
Proteins: Structure, Function and Genetics, 2004