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Volume 17, Issue 11
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

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.

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/content/journals/ppl/10.2174/0929866511009011363
2010-11-01
2025-05-24

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

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