PubMed · 15408708
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C A MILLS. 1950-01-20. The Denora episode.. https://doi.org/10.1126/science.111.2873.67
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Physicochemical properties of PBLG (poly(gamma-benzyl-l-glutamate))-PEO (poly(ethylene oxide)) diblock copolymers composed of PBLG as the hydrophobic rod component and PEO as the hydrophilic component were investigated at the air-water interface. Surface pressure-area isotherms obtained by the Wilhelmy plate method provide several variables such as molecular size, compressibility of PEO, and the free energy change of the PBLG-PEO block copolymer. GE-1 (M(w) of PBLG:PEO=103,700:12,000), with a relatively longer rod, has negative temperature effects and GE-3 (M(w) of PBLG:PEO=8400:12,000), with a relatively shorter rod, shows a positive temperature effect because of the large entropy loss. These competitions were based on the block size of PBLG and PEO and were affected by various microstructures of the PBLG-PEO diblock copolymer. Monolayer aggregations transferred onto mica from the air-water interface were analyzed with AFM. AFM images of GE-1 monolayers show cylindrical micelles, but the self-assembled structure has many large domains. The monolayer of GE-2 (M(w) of PBLG:PEO=39,800:12,000), which has a medium size rod, forms a spherical structure at the air-water interface. Monolayers of GE-3, with a short rod length, form bilayer structures. These results demonstrate that the microstructures of PBLG-PEO diblock copolymers are related to free energy changes between rod and coil blocks.
In this study, we investigated the interaction of fengycin, a lipopeptide produced by Bacillus subtilis, with lipid monolayers using the Langmuir trough technique in combination with Brewster angle microscopy. Thermodynamic analyses were performed to get further information about the mixing behavior and the molecular interactions between the two components. The effect of fengycin on the structural and morphological characteristics of DPPC monolayers, as a simple model of biological membranes, depends on the fengycin molar ratio. With a small proportion of fengycin (X(f)0.1), the compressibility of the monolayer is modified but the morphological characteristics of the DPPC are not significantly affected. At an intermediate molar ratio (0.1<X(f)0.5), fengycin has a fluidizing effect on the DPPC monolayer by interacting partially with DPPC molecules. At higher molar ratio (X(f)=0.66), fengycin totally dissolves the ordered phase of the lipid. These results highlight the capacity of fengycin to perturb the DPPC organization and are discussed in relation to fengycin capacity to affect biological membranes.
In this study, we discuss the interfacial behavior of five proteins with different conformational character, and each is investigated in native and denatured states. The protein molecules are layered and spread onto the air/solution interfaces to form protein monolayer. The surface pressure-time (Pi(t)) and surface pressure-area per molecule (Pi-A) isotherms were measured by using the Langmuir-Blodgett (LB) balance consisted of a Nima trough system. The differences between monolayered protein's behaviors at air/solution interface indicate that denaturants, such as urea, guanidinium chloride and dithiothreitol, have different effects on conformational changes of proteins. Additionally, the interfacial behavior of the proteins in our study provides a fundamental profile about the protein structural stability and implies industrial applications in protein refolding process.