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• W2030661166 abstract "Abstract Alamethicin, melittin, protein kinase C (PKC) and phospholipase A2 ame amphipatic molecules and tend to adsorb through their hydrophobic residues, on hydrophobic mercury electrode surfaces, at around zero charge potentials. During adsorption, the differential capacity of the electrical double layer is lowered to around 4 μF cm2 by alamethicin, to 7 μF cm2 by PKC, and to 8.5 μF cm2 by melittin. The limiting area of the adsorbed alamethicin as obtained from the diffusion controlled kinetics is 2.6 ± 0.2 nm2. The limiting area of melittin could not be obtained by this method as its adsorption was slowed down by the electrostatic repulsion between the positively charged adsorbing molecule and the already adsorbed monolayer. Ultimately its saturated monolayer was less dense than that of alamethicin. Adsorbed PKC exhibits pseudocapacitance peaks at up to three different potentials owing to oxyreduction of cystine residues in different domains with different proton activity, while phospholipase A2 has only one pseudocapacitance peak. All the polypeptides and proteins investigated perturb the structure of the lipid monolayer at the mercury—water interface, making it more permeable to ionic redox agents as detected by their pseudocapacitance peaks. However, no channels across the monolayers are formed. The perturbation of the lipid monolayers by PKC and phosphotipase A2 is also indicated by the cystine redox pseudocapacitance peaks. In the case of PKC the perturbation of the lipid structure is enhanced by diacylglycerol (DAG) and by phorbol ester (TPA)." @default.
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• W2030661166 date "1992-08-01" @default.
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• W2030661166 title "Interaction of alamethicin, melittin and protein kinase C with pure and phospholipid monolayer covered mercury electrode surfaces" @default.
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• W2030661166 doi "https://doi.org/10.1016/0022-0728(92)85079-i" @default.
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