Formation of complexes between protein particles and long amphiphilic polymers: binding isotherms versus size and surface of the particles

Article Abstract:

The interaction between hydrophobically modified polyacrylates (HMPA) and serum albumins was investigated. Binding isotherms were obtained using frontal analysis continuous capillary electrophoresis. The main qualitative features of this association were anticooperativity, high sensitivity to the hydrophobicity of HMPAs, no sensitivity to the size of the proteins, and subtle differences related to small variations in primary structure. Isotherms appeared to be not markedly dependent on protein size in terms of molar ratio.

Research, Usage, Electrophoresis, Protein binding, Serum albumin, Complex compounds, Coordination compounds, Acrylates

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Effect of temperature and chemical modification on polymer Langmuir films

Article Abstract:

Surface pressure-area (PI-A) isotherms and interfacial shear rheology experiments were performed to better understand the effects of two modifications, namely, varying the temperature between 5 and 40 degrees Celsius and introducing small amounts of carboxylic acid groups by partially hydrolyzing the polymer. Results reveal that both of these modifications can change the interactions that govern the shape of the surface pressure-area isotherm and interfacial rheological properties.

Analysis, Thin films, Multilayered, Multilayered thin films, Hydrolysis, Structure, Chemical properties, Methacrylates, Tertiary butyl compounds

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