Abstract

The Langmuir Blodgett apparatus provides a versatile system for studying the interfacial properties of peptides and peptide-membrane interactions under controlled conditions. Using amphiphilic α-helical peptides to highlight studies undertaken, here we discuss the use of this system to provide information on the surface activity of peptides and describe the insights these studies give into biological function.

Keywords: Amphiphilic peptide, langmuir blodgett, maximum surface pressure, monolayer, phospholipid, thermodynamic analysis, peptide, langmuir, maximum, thermodynamic, helices, (IEP), anticancer peptides, AMPHIPHILIC PEPTIDES, Escherichia coli, pH, adsorption, AMPs, melittin, SIKVAV, constant area as-say, constant pressure assay, compression isotherm analysis, (DPPG), (DPPC), (PG), (CL), Gram-negative bacteria, (LPS), bilayer, (DMPS), (PC)(SM), (PE), (DOPC), (DOPG), (LE), (LC), (BAM), (AFM), IEP, AcVP3110, (POPC), (DEPC)