Binding of cationic pentapeptides with modified side chain lengths to negatively charged lipid membranes: Complex interplay of electrostatic and hydrophobic interactions

Article ID	Journal	Published Year	Pages	File Type
10797339	Biochimica et Biophysica Acta (BBA) - Biomembranes	2012	10 Pages	PDF

Abstract

âº Binding of Lys5 analogs with shorter side chains to anionic lipid membranes. âº ITC, DSC, IR_spectroscopy and monolayer techniques were used for binding studies. âº Hydrophobic spacers of the side chains contribute to binding. âº Discrimination between electrostatic and hydrophobic contributions to binding.

Keywords

DAB DSC myristoylated alanine-rich C-kinase substrate POPG DPPG DMPG PLL ORN DAP ITC MARCKS TFA 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol Arginine Peptide binding Arg Trifluoroacetic acid ornithine Electrostatic interaction Hydrophobic interaction FT-IR phosphatidyl glycerol Fourier-transform infrared Lysine LYS Pentapeptide Isothermal titration calorimetry Differential scanning calorimetry