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- W2059403905 abstract "Melittin, the main peptide component of European Honey Bee venom, is a 26-amino acid peptide that permeabilizes bacterial and mammalian cells, as well as synthetic lipid vesicles. Melittin is one of the most studied pore forming peptides, and researchers hold it as a framework for designing engineered peptides pores. We have sought to optimize the potency of melittin, by applying orthogonal high throughput screen strategies to select for gain-of-function analogs of melittin. Here we use electrochemical impedance spectroscopy (EIS) to compare the activity of melittin and one gain-of-function melittin analogue. While EIS studies of melittin show a decrease in admittance with a transient recovery we find a strikingly different bilayer response to the melittin analogue- an exponential decay with a half-life of 15-30 seconds. These experiments demonstrate the remarkable ability of the gain-of-function melittin analogue to form stable pores on lipid bilayers. Thus the engineered analogues have many applications in biotechnology and as anti-cancer therapeutics." @default.
- W2059403905 created "2016-06-24" @default.
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- W2059403905 date "2012-01-01" @default.
- W2059403905 modified "2023-09-28" @default.
- W2059403905 title "Effect of Melittin and Gain-of-Function Melittin Analogs, Discovered by High-Throughput Screening, on Bilayer Properties: An Electrical Impedance Spectroscopy Study" @default.
- W2059403905 doi "https://doi.org/10.1016/j.bpj.2011.11.517" @default.
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