Molecular aspects of the biological mechanism of action of the synthetic peptide HFRWPGP, including an assessment of the stability to membrane proteolytic enzymes and the determination of several intermolecular interaction parameters of the peptide and rat-brain cytoplasmic membranes. It was hypothesized based on the results that the peptide apparently acts as an allosteric activity modulator for several receptor systems and can after the nature of signal transfer to cells. It was established that heptapeptide HFRWPGP in the presence of cerebellum and hippocampus cytoplasmic membranes was degraded in a manner similar to that of Semax proteolysis (used as a reference peptide) under the same incubation conditions.
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Acknowledgments
The work was supported in part by the RAS Presidium Basic Research Program “Molecular and Cellular Biology,” State Reg. No. 01201353020 and a Grant for Scientific Schools No. 14.120.14.4222-NSh under the direction of Akad. N. F. Myasoedov.
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Translated from Khimiko-Farmatsevticheskii Zhurnal, Vol. 51, No. 5, pp. 9 – 12, May, 2017.
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V’yunova, T.V., Shevchenko, K.V., Andreeva, L.A. et al. Enzymatic Stability and Possible Molecular Targets of Synthetic Peptide HFRWPGP. Pharm Chem J 51, 337–339 (2017). https://doi.org/10.1007/s11094-017-1609-0
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DOI: https://doi.org/10.1007/s11094-017-1609-0