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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

A Langmuir Approach Using Monolayer Interactions to Investigate Surface Active Peptides

Author(s): Sarah R. Dennison, Frederick Harris and David A. Phoenix

Volume 17, Issue 11, 2010

Page: [1363 - 1375] Pages: 13

DOI: 10.2174/0929866511009011363

Price: $65

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)


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