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Mendeleev Communications, 2022, Volume 32, Issue 4, Pages 436–438
DOI: https://doi.org/10.1016/j.mencom.2022.07.003
(Mi mendc687)
 

This article is cited in 1 scientific paper (total in 1 paper)

Communications

The neuropeptide cycloprolylglycine can form a complex with AMPA receptors

V. Kh. Akparova, V. I. Timofeevb, K. N. Koliasnikovac

a National Research Centre 'Kurchatov Institute', Moscow, Russian Federation
b A.V. Shubnikov Institute of Crystallography, FSRC ‘Crystallography and Photonics', Russian Academy of Sciences, Moscow, Russian Federaion
c V.V. Zakusov Research Institute of Pharmacology, Moscow, Russian Federation
Full-text PDF (401 kB) Citations (1)
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.
Keywords: allosteric site of AMPA receptor, endogenous ampakine, cycloprolylglycine, piracetam, MM-GBSA.
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Document Type: Article
Language: English


Citation: V. Kh. Akparov, V. I. Timofeev, K. N. Koliasnikova, “The neuropeptide cycloprolylglycine can form a complex with AMPA receptors”, Mendeleev Commun., 32:4 (2022), 436–438
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