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Interactions of Proteins with Polymers

Reception of chemical and biochemical signals can be based on a physical interaction or chemical reaction between functional groups in the polymer and signaling molecules (Motomov et al. 2010). There are many examples of specific complex formation between synthetic polymer materials and ligands, e.g., glucose-responsive polymers with phenylboronic side groups (Lapeyre et al. 2008). [Pg.740]

Nuclear Magnetic Resonance Studies of Interfacial Phenomena [Pg.742]

Nanosilica A-300 and A-50 S =232 or 297 and 52 mVg, respectively) was heated at 673 K for several hours to remove residual HCl and other adsorbed compounds (Gun ko et al. 2006i). Proteins such as BSA ( Allergen, Stavropol, Russia, molecular weight Wm 67 kDa), gelatin (Merck, powder food grade), ovalbumin (Wm 44 kDa), and ossein ( Indar, Kiev, Ukraine, 24.5 4.5 kDa) polymers such as PVP ( Biopharma, Kiev, 12.6 2.7 kDa), PVA ( Stirol, Severodonetsk, Ukraine 43 7 kDa), and PEG (Flnka, BV 2, 20 and 35 kDa) were used in QELS experiments to analyze the kinetic interactions of co-adsorbates (Gun ko et al. 2006i). [Pg.742]

Before adsorption of polymers, nanosUica S =232 mVg) was heated in air at 450°C for several hours to remove adsorbed compounds. Certain amounts of the nanosilica powder and a polymer (PVP or PEG) solution were loaded into a glass reactor (2 dm ) with a mixer ( 500 rpm) providing a pseudo-liquid state (PLSR) of a powder and agitated at room temperature for 0.5 h. Then certain amount of ethanol was dripped (one or two drops per second) in the reactor at room temperature and the mixture was agitated for 1-6 h, and then it was dried at room temperature (Gun ko et al. 2006i). [Pg.742]

DLS investigations were performed using a Zetasizer 3000 (Malvern Instruments) apparatus (A,=633 nm, 0=90°) at 298 K (Gun ko et al. 2006i). Deionized distilled water was used for preparation of nanosilica suspension (CsiO2=0.1 and 0.5 wt% for the systems based on A-300 and [Pg.742]


Application of the vOCG Theory to the HydrophilicjHydrophobic Interactions of Proteins with Polymer Surfaces... [Pg.117]


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