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Controlled uptake and release of proteins by polyelectrolyte gels
Author(s) -
Zezin A.,
Rogacheva V.,
Skobeleva V.,
Kabanov V.
Publication year - 2002
Publication title -
polymers for advanced technologies
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.61
H-Index - 90
eISSN - 1099-1581
pISSN - 1042-7147
DOI - 10.1002/pat.244
Subject(s) - polyelectrolyte , sorption , ionic strength , desorption , salt (chemistry) , chemical engineering , aqueous solution , ionic bonding , kinetics , polymer chemistry , materials science , chemistry , chromatography , polymer , ion , organic chemistry , adsorption , physics , quantum mechanics , engineering
The equilibrium and kinetics of proteins sorption and desorption by oppositely charged lightly crosslinked polyelectrolytes (#PE) were studied. The driving force of the sorption is provided by interpolyelectrolyte addition reaction (IPAR) between oppositely charged ionic groups of protein and #PE resulting in protein–#PE complex (#PPEC) formation. The capacity of different #PEs with respect to the proteins in neutral salt‐free aqueous solutions is rather high, exceeding that of the known heterogeneous crosslinked polyelectrolyte sorbents commonly used for protein sorption in practice. The dependence of the capacity of #PE on pH and the salt concentration in the environmental solution has been revealed and investigated. The equilibrium of IPAR is shifted to the original components under the corresponding pH shift or adding a simple salt. As a result the protein releases into the surrounding solution. The rate of protein uptake and release is also controlled by the pH or/and the ionic strength of the solution. The data obtained show that #PE can be used to design the crosslinked polyelectrolyte constructs for controlled uptake and release of proteins. Copyright © 2003 John Wiley & Sons, Ltd.