Understanding non-cognate and cognate protein -polyelectrolyte interactions
Abstract
Electrostatic features of both non-cognate and cognate protein-GAG systems were investigated to give a better insight into the binding of a diverse set of proteins to these highly heterogeneous polyelectrolytes and. The pH and ionic strength dependence of the binding constants and the significance of protein electrostatic potential distributions and charge anisotropy indicate some general features of non-specific electrostatic interactions. The paradigmatic cognate pair antithrombin (AT) and heparin (Hp) was studied to investigate the relevance of such non-specific electrostatic contributions to this "specific binding" interaction. The interaction of Hp and AT displays several of the features characteristic of "non-specific" protein-polyelectrolyte complexation. The AT binding of a low molecular weight Hp (LMWH) sample was investigated by capillary electrophoresis, affinity chromatography, FACCE, and SEC-MS of LMWH affinity fractions. The results are not consistent with the commonly held viewpoint that AT binds only to a unique pentasaccharide sequence within Hp.
Degree
Ph.D.
Advisors
Dubin, Purdue University.
Subject Area
Chemistry
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