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A Langmuir Approach Using Monolayer Interactions to Investigate Surface Active Peptides

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

Document Type: Research Article

Publication date: 2010-11-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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