Abstract
It is shown using small-angle X-ray scattering (SAXS) that the tetrapeptide, which is an inductor of fibrillogenesis for a fragment of α-human lactalbumin β-domain, is active in the form of supramolecular complexes. Formation of these complexes was not detected by microscopy and analytical gel filtration. Molecular-dynamics simulation of the behavior of an ensemble of tetrapeptides using the free diffusion method confirmed their experimentally observed tendency to form oligomers. The obtained data and methodical approaches can be applied to develop new peptide drugs, which can modulate the activity of proteins by affecting their spatial structure.
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ACKNOWLEDGMENTS
The SAXS curves were obtained at the European Synchrotron Radiation Facility (Grenoble, France), experiment no. LS2508 @ID02.
Funding
This study was supported by the National Research Centre “Kurchatov Institute” (order no. 1363, dated June 25, 2019).
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Translated by Yu. Sin’kov
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Zabrodskaya, Y.A., Shvetsov, A.V., Garmay, Y.P. et al. Supramolecular Complexes of Tetrapeptides Capable of Inducing the Human α-Lactalbumin β-Domain Conformational Transitions. Crystallogr. Rep. 66, 840–845 (2021). https://doi.org/10.1134/S1063774521050254
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DOI: https://doi.org/10.1134/S1063774521050254