Tunable Encapsulation of Proteins within Charged Microgels.

ABSTRACT: 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 × 10(5) cytochrome c molecules per particle. Binding resulted in the formation of a polymer-protein complex and condensat

SUBMITTER: Smith MH 

PROVIDER: S-EPMC3207277 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature