Phospholipid headgroup

Tb "" - RITC-DPPE Ca site is 10 A from phospholipid headgroup 412... 

For pure phosphatidylcholine bilayers, the orientation of the headgroup has been well characterized showing that headgroups are aligned approximately parallel to the bilayer surface. Because only one phosphorus with 100% natural abundance is contained in the phospholipid molecule, NMR has become an important tool to study the phospholipid headgroup structure and dynamics. ... 

The interface between the polar phospholipid headgroups and the aqueous electrolyte solution provides a membrane surface which contains weakly selective cationic binding sites. (10) This generates a reservoir of cations available for conduction and is apparently much more important than bulk solution Ion content in the determination of permion and ion current density. (11)... 

Moghimi, S. M., and Hunter, A. S. (2001), Recognition by macrophages and liver cells of opsonized phospholipid vesicles and phospholipid headgroups, Pharm. Res., 18, 1-8. 

The SLB is conventionally formed on silica surfaces and stabilized by interactions between the hydrophilic hydroxyl surface and the phospholipid headgroups. It is purely a phospholipid bilayer stabilized only by electrostatics and the hydrophobic... 

Density profile for water, trehalose, and phospholipid headgroups (nitrogen and phosphorous) for a fully hydrated DPPC bilayer. Simulations at 50°C indicate that trehalose concentration is higher near phospholipid head groups than in the bulk (FaUer et al., 2003). The concentration of trehalose in the aqueous phase is 4% by weight. 

Kinney, A.J. 1993. Phospholipid headgroups. In Upid Metabolism in Plants. T.S. Moore, Jr., editor. Boca Raton, FL CRC Press, pp. 259-284. 

This protocol describes the preparation and attachment of histidine-tagged proteins to the bilayers containing Ni-NTA in the phospholipid headgroups. The main advantage of this technique is that the genetic fusion of the histidine tag with the protein results in a predictable orientation of the protein on the bilayer and maintains protein s natural stoichiometry. Alternatively, proteins can also be attached to lipid bilayers covalently, or by a streptavidin-biotin linkage, but these techniques can result in random orientation and multimerization of the proteins. 

Much data have now shown that peptides, proteins, and lipids exhibit antimicrobial activity. The selective toxicity of peptides toward bacterial cells is primarily due to an initial electrostatic interaction between the peptide and the anionic phospholipid headgroups in the outer leaflet of the bacterial cytoplasmic membrane (Zasloff, 1987 Yeaman and Yount, 2003). A diversity of antimicrobial peptide sequences and structures have been discovered (Yeaman and Yount, 2003 Lai and GaUo, 2009), and this diversity underscores the reality that no single antimicrobial peptide sequence has emerged as an effective antimicrobial. Furthermore, the diversity of molecules as antimicrobials may be an evolutionary strategy to prevent or delay the development of microbial resistance to antimicrobial peptides. 

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