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Tunable Encapsulation of Proteins within Charged Microgels

The binding of cytochrome c to pH and thermoresponsive colloidal hydrogels was investigated using multiangle light scattering, measuring loading through changes in particle molar mass and root-mean-square radius. Loosely cross-linked microgels [composed of a random copolymer of N-isopropylacrylamide (NIPAm) and acrylic acid (AAc)] demonstrated a high loading capacity for protein. Encapsulation was dependent on both the charge characteristics of the network and the salinity of the medium. Under favorable binding conditions (neutral pH, low ionic strength), microgels containing the highest studied charge density (30 mol % AAc) were capable of encapsulating greater than 9.7 × 105 cytochrome c molecules per particle. Binding resulted in the formation of a polymer–protein complex and condensation of the polymer. Anionic microgels demonstrated a change in density ∼20-fold in the presence of oppositely charged proteins. These studies of cytochrome c encapsulation represent a significant step toward direct measur...

Authors:   Michael H. Smith; L. Andrew Lyon
Journal:   Macromolecules
Year:   2011
DOI:   10.1021/ma201365p
Publication date:   18-Oct-2011
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