The peculiarity of ion transport at the nanoscale is revealed through electrophysiological studies of two biological ion channels: the cation-selective bacterial porin-OmpF and the mitochondrial voltage-dependent anion channel (VDAC). We provide evidence of an unprecedented scaling behavior in the power-law relationship between conductivity and concentration ∼ with > 1 when functional groups attached to the pore inner wall have opposite charges to those located in the nanochannel's outer surface. Indeed, we find ∼ 1.
View Article and Find Full Text PDFDynorphin A (DynA) is an endogenous neuropeptide that besides acting as a ligand of the κ-opioid receptor, presents some non-opioid pathophysiological properties associated to its ability to induce cell permeability similarly to cell-penetrating peptides (CPPs). Here, we use electrophysiology experiments to show that amphiphilic DynA generates aqueous pores in neutral membranes similar to those reported previously in charged membranes, but we also find other events thermodynamically incompatible with voltage-driven ion channel activity (i.e.
View Article and Find Full Text PDFIon permeation across nanoscopic structures differs considerably from microfluidics because of strong steric constraints, transformed solvent properties, and charge-regulation effects revealed mostly in diluted solutions. However, little is known about nanofluidics in moderately concentrated solutions, which are critically important for industrial applications and living systems. Here, we show that nanoconfinement triggers general biphasic concentration patterns in a myriad of ion transport properties by using two contrasting systems: a biological ion channel and a much larger synthetic nanopore.
View Article and Find Full Text PDFAlthough nanoplastics have well-known toxic effects toward the environment and living organisms, their molecular toxicity mechanisms, including the nature of nanoparticle-cell membrane interactions, are still under investigation. Here, we employ dynamic light scattering, quartz crystal microbalance with dissipation monitoring, and electrophysiology to investigate the interaction between polystyrene nanoparticles (PS NPs) and phospholipid membranes. Our results show that PS NPs adsorb onto lipid bilayers creating soft inhomogeneous films that include disordered defects.
View Article and Find Full Text PDFDynorphins 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.
View Article and Find Full Text PDFAdsorption processes are central to ionic transport in industrial and biological membrane systems. Multivalent cations modulate the conductive properties of nanofluidic devices through interactions with charged surfaces that depend principally on the ion charge number. Considering that ion channels are specialized valves that demand a sharp specificity in ion discrimination, we investigate the adsorption dynamics of trace amounts of different salts of trivalent cations in biological nanopores.
View Article and Find Full Text PDFMicro- (<5 mm) and nanoplastics (<1 μm) are emerging threats for marine ecosystems worldwide. Brine shrimp Artemia is recognized as a suitable model among planktonic species for studying the impact of polystyrene nanoparticles (PS NPs) through short and long-term bioassays. Our study aims to evaluate the time-dependent effects of cationic amino-modified PS-NH (50 nm) in A.
View Article and Find Full Text PDFThe outer membrane of Gram-negative bacteria contains β-barrel proteins that form high-conducting ion channels providing a path for hydrophilic molecules, including antibiotics. Traditionally, these proteins have been considered to exist only in an open state so that regulation of outer membrane permeability was accomplished via protein expression. However, electrophysiological recordings show that β-barrel channels respond to transmembrane voltages by characteristically switching from a high-conducting, open state, to a so-called 'closed' state, with reduced permeability and possibly exclusion of large metabolites.
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