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- W4200494060 abstract "Dynorphins are endogenous neuropeptides that function as ligands for the κ-opioid receptor. In addition to opioid activity, dynorphins can induce several pathological effects such as neurological dysfunctions and cell death. Previous studies have suggested that Dynorphin A (DynA) mediates some pathogenic actions through formation of transient pores in lipid domains of the plasma membrane. Here, we use planar bilayer electrophysiology to show that DynA induces pore formation in negatively charged membranes. We find a large variability in pore conformations showing equilibrium conductance fluctuations, what disregards electroporation as the dominant mechanism of pore formation. Ion selectivity measurements showing cationic selectivity indicate that positive protein charges of DynA are stabilized by phosphatidyl serine negative charges in the formation of combined structures. We complement our study with computational simulations that assess the stability of diverse peptide arrangements in the hydrophobic core of the bilayer. We show that DynA is capable of assembling in charged membranes to form water-filled pores that conduct ions." @default.
- W4200494060 created "2021-12-31" @default.
- W4200494060 creator A5038294482 @default.
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- W4200494060 creator A5064543345 @default.
- W4200494060 creator A5066763612 @default.
- W4200494060 creator A5079361196 @default.
- W4200494060 date "2022-01-01" @default.
- W4200494060 modified "2023-10-18" @default.
- W4200494060 title "Dynorphin A induces membrane permeabilization by formation of proteolipidic pores. Insights from electrophysiology and computational simulations" @default.
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- W4200494060 doi "https://doi.org/10.1016/j.csbj.2021.12.021" @default.
- W4200494060 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35024095" @default.
- W4200494060 hasPublicationYear "2022" @default.
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