Surface charge proteins

A good example of a surface-modified lens is the Sola/Bames-Hind Hydrocurve Flite lens, introduced in 1986. The material for the commercial Hydrocurve lens, bufilcon A [56030-52-5] contains methacrylic acid and has a high affinity for protein and subsequent deposition. The surface of the Flite lens was chemically modified with the addition of diazomethane (190) to reduce the surface charge. In vitro testing demonstrated a decrease in protein adsorption (191). 

Preparation of nanoparticles can be by a variety of different ways. The most important and frequently used is emulsion polymerization others include interfacial polymerization, solvent evaporation, and desolvation of natural proteins. The materials used to prepare nanoparticles are also numerous, but most commonly they are polymers such as poly-alklcyanoacrylate, polymethylmethacrylate, poly-butylcyanoacrylate, or are albumin or gelatin. Distribution patterns of the particles in the body can vary depending on their size, composition, and surface charge [83-85]. In particular, nanoparticles of polycyanoacrylate have been found to accumulate in certain tumors [86,87]. 

Clay minerals or phyllosilicates are lamellar natural and synthetic materials with high surface area, cation exchange and swelling properties, exfoliation ability, variable surface charge density and hydrophobic/hydrophilic character [85], They are good host structures for intercalation or adsorption of organic molecules and macromolecules, particularly proteins. On the basis of the natural adsorption of proteins by clay minerals and various clay complexes that occurs in soils, many authors have investigated the use of clay and clay-derived materials as matrices for the immobilization of enzymes, either for environmental chemistry purpose or in the chemical and material industries. 

The number and the type of amino acids and their sequence determine the surface charge of the protein, its molecular configuration and its unique chemical and physical properties. The function of a protein is dependent on its three-dimensional structure. A number of agents can dismpt this structure thus denaturing it, for example changes in pH, temperature, salt concentration, and the presence of reducing substances. 

As depicted in Fig. 5, both the protein molecule and the sorbent surface are electrically charged. In an aqueous environment, they are surrounded by counterions, which, together with the surface charge, form the so-called electrical double layer. The Gibbs energy of an electrical double layer, may be calculated as the isothermal, isobaric reversible work required to invoke the charge distribution in the double layer... 

The sorbent materials are supplied as finely dispersed colloidal particles, whose surfaces are smooth. Some of their properties are presented in Table 3. The sorbents cover different combinations of hydrophobicity and sign of the surface charge. Thus, the model systems presented allow systematic investigation of the influences of hydrophobicity, electric charge, and protein structural stability on protein adsorption. 

Differences in protein surface charge at a given pH Differences in mass/shape of different proteins Based upon biospecific interaction between a protein and an appropriate ligand... 

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