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- W2007643170 abstract "The biophysical characteristics of synthetic, naturally occurring peptides forming membrane-spanning channels were investigated by using isolated rod outer segments (OS) of frog, recorded in whole-cell configuration. The peptides were applied to (and removed from) the OS in ∼50 ms with a computer-controlled microperfusion system. Once blocking the main OS endogenous conductance (the cGMP channels) with saturating light, the OS membrane resistance was mostly >1 GOhm. In symmetric K or Na, 1 µM synthetic alamethicin F50/5 produced a current after ∼0.21 s from the solution exchange (called Delay), that activated monoexponentially (time constant τa∼0.26 s) to a maximal amplitude (Imax) of ∼700 pA. Peptide removal caused the current to return to 0, with a non-measurable Delay, and again monoexponentially (time constant τd∼0.31 s), showing the full reversibility of the permeabilization process. Imax, Delay, τa, and τd of current produced by 1 µM of [L-Glu(OMe)7,18,19] (where the Gln 7,18,19 were substituted with side-chain esterified Glu residues) were respectively similar, ∼8-fold, ∼16-fold, and ∼6-fold larger than those of alamethicin F50/5. For both peptides, the current-to-voltage characteristics (obtained with voltage ramps) showed a strong inward rectification at early times of application; current was carried equally well by monovalent and divalent cations. However, activation kinetics accelerated more than 100-fold if external Na or K was substituted with an equiosmolar amount of Ca in the case of F50/5, but up to 10-fold in the case of [L-Glu(OMe)7,18,19]; Delay and τd were not significantly affected by divalent cations. Similar results were preliminarily obtained in the presence of Mg or Mn, indicating that the effect of divalent cations was not due to a change in the surface charge density of plasma membrane, but to an increase of probability of pore formation." @default.
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- W2007643170 date "2010-01-01" @default.
- W2007643170 modified "2023-09-28" @default.
- W2007643170 title "Divalent Cations Regulate Pore Formation of Synthetic, Naturally Occurring Alamethicin and Selected Analogs" @default.
- W2007643170 doi "https://doi.org/10.1016/j.bpj.2009.12.597" @default.
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