Abstract:
:Turbidimetric titration was used to initiate associative intermolecular interactions between a pair of protein molecules, gelatin-A and gelatin-B, having complementary charges that led to pH-induced liquid-liquid phase separation and the formation of complex coacervate. The stoichiometric binding ratio was found to be [gelatin-A]/[gelatin-B]=3:2. The size of soluble intermolecular aggregates present in the supernatant exhibited interesting time-dependent coacervation because of residual electrostatic interactions. Dynamic light scattering and turbidity studies provided a systematic account of coacervation behavior. Rheology studies attributed the softening of the coacervate matrix to the presence of encapsulated salbutamol sulfate. The in vitro drug release kinetics was probed in simulated gastric fluid medium at physiological temperature (37 degrees C), which showed biphasic behavior. The initial release kinetics exhibited an exponential growth to saturation behavior, followed by a slower logarithmic release process.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Tiwari A,Bindal S,Bohidar HBdoi
10.1021/bm801160ssubject
Has Abstractpub_date
2009-01-12 00:00:00pages
184-9issue
1eissn
1525-7797issn
1526-4602pii
10.1021/bm801160sjournal_volume
10pub_type
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