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• W2912472890 abstract "Abstract How is a water-soluble globular protein able to spontaneously cross a cellular membrane? It is commonly accepted that it undergoes significant structural rearrangements on the lipid-water interface, thus acquiring membrane binding and penetration ability. In this study molecular dynamics (MD) simulations have been used to explore large-scale conformational changes of the globular viscumin A chain in a complex environment – comprising urea and chloroform/methanol (CHCl 3 /MeOH) mixture. Being well-packed in aqueous solution, viscumin A undergoes global structural rearrangements in both organic media. In urea, the protein is “swelling” and gradually loses its long-distance contacts, thus resembling the “molten globule” state. In CHCl 3 /MeOH, viscumin A is in effect turned “inside out”. This is accompanied with strengthening of the secondary structure and surface exposure of hydrophobic epitopes originally buried inside the globule. Resulting solvent-adapted models were further subjected to Monte Carlo simulations with an implicit hydrophobic slab membrane. In contrast to only a few point surface contacts in water and two short regions with weak protein-lipid interactions in urea, MD-derived structures in CHCl 3 /MeOH reveal multiple determinants of membrane interaction. Consequently it is now possible to propose a specific pathway for the structural adaptation of viscumin A with respect to the cell membrane – a probable first step of its translocation into cytoplasmic targets." @default.
• W2912472890 created "2019-02-21" @default.
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• W2912472890 date "2019-01-23" @default.
• W2912472890 modified "2023-09-26" @default.
• W2912472890 title "Specific refolding pathway of viscumin A chain in membrane-like medium reveals a possible mechanism of toxin entry into cell" @default.
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• W2912472890 doi "https://doi.org/10.1038/s41598-018-36310-6" @default.
• W2912472890 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6344525" @default.
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• W2912472890 hasPublicationYear "2019" @default.
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