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Conformational Dynamics of Poly(acrylic acid)‐Bovine Serum Albumin Polycomplexes at Different pH Conditions
Author(s) -
Akkilic Namik,
Mustafaev Mamed,
Chegel Volodymyr
Publication year - 2008
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.200850917
Subject(s) - bovine serum albumin , polyelectrolyte , acrylic acid , surface plasmon resonance , chemistry , macromolecule , polymer chemistry , polymer , fluorescence , serum albumin , conformational change , biophysics , crystallography , stereochemistry , materials science , organic chemistry , chromatography , copolymer , biochemistry , nanotechnology , physics , quantum mechanics , nanoparticle , biology
This work presents the real time surface plasmon resonance (SPR) and fluorescence spectroscopy observation of cooperative interactions between aggregate‐forming bovine serum albumin (BSA) and oppositely charged linear macromolecule poly(acrylic) acid (PAA). Interactions between protein and polymer result in formation of polyelectrolyte‐protein polycomplexes, which exhibit expressed conformational transformations, especially at low pH. The rate constants of observed kinetic transformations were calculated and found to vary in the range from 0.8 × 10 −3 to 6.7 × 10 −3 for different pH values. The processes of aggregation, sedimentation and conformation of BSA‐PAA complex are discussed.