A thermodynamic approach to alamethicin pore formation
نویسندگان
چکیده
منابع مشابه
Pore formation in lipid membranes by alamethicin.
The conformation of the linear peptide antibiotic alamethicin in dipalmitoyl phosphatidylcholine multilayers was investigated in the absence of an electric field by means of infrared attenuated total reflection spectroscopy. Alamethicin was found to be incorporated into the lipid membrane not only in the dry state but also in an aqueous environment. Its molecular conformation, however, changed ...
متن کاملAlamethicin-induced pore formation in biological membranes.
The effects of alamethicin on the membrane barrier function of rabbit erythrocytes, human platelets and sarcoplasmic reticulum vesicles, as well as on that of brain microsomes and liver mitochondria of the rat were compared. An upset of the barrier function was observed for plasma membranes of brain microsomes as well as for erythrocyte and platelet membranes at alamethicin concentrations rangi...
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A new ohmic contact scheme for gallium nitride is presented. The use of Nitrideforming metal Over Gallide-forming metal, “NOG”, can modify the thermodynamic activity of N and Ga near the interface. This in turn can modify the near-surface point defect concentrations, particularly the vacancies of Ga and N. The principle of this contact scheme was shown to be consistent with results from Ni/Au, ...
متن کاملContinuum solvent model calculations of alamethicin-membrane interactions: thermodynamic aspects.
Alamethicin is a 20-amino acid antibiotic peptide that forms voltage-gated ion channels in lipid bilayers. Here we report calculations of its association free energy with membranes. The calculations take into account the various free-energy terms that contribute to the transfer of the peptide from the aqueous phase into bilayers of different widths. The electrostatic and nonpolar contributions ...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2014
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2014.01.012