Structural organization of alpha-helical peptide antibiotic alamethicin at the air/water interface

Article Abstract:

The structural organizations of Lanmuir monolayers of the alpha-helical peptide alamethicin, which forms voltage-gated ion channels in lipid membranes, is studied y means of synchrotron X-ray diffraction, surface potential technique, surface pressure/area isotherms, and atomic force microscopy (AFM). The effects of hydrogen-bond promoters, pH, salt content of the aqueous sub phase, and lipid-peptide interactions were also analyzed.

Proteins, X-ray diffraction, Protein structure, Atomic force microscopy

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Lipophilicity of peptide anions: An experimental data set for lipophilicity calculations

Article Abstract:

The standard Gibbs energies of the transfer of peptide anions from aqueous solution to nitrobenzene are determined with the help of electrochemical measurements. The study indicate that the lipohilicity contributions of single amino acid residues to the overall lipohilicity of a peptide anion strongly depend on the position of the amino acid in the backbone of the peptide.

Electric properties, Energy transfer, Gibbs' free energy

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A comparison of the solvation properties of 2-nitrophenyloctyl ether, nitrobenzene, and n-octanol as assessed by ion transfer experiments

Article Abstract:

The lipophilicity data of a number of anions of drugs and model compounds are determined at the water-nitrophenyloctyl ether (NPOE) and water-nitrobenzene (NB) interfaces by using the three-phase electrode approach. For both inorganic and organic anions it appears that NPOE is more similar to NB than to n-octanol.

All Other Basic Organic Chemical Manufacturing, Industrial Organic Chemicals, Cyclic crudes and intermediates, Cyclic Crude and Intermediate Manufacturing, Nitrobenzene, Octanol, Ether, Ether (Anesthetic), Nitrobenzenes, Chemical properties

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