ABSTRACT
Intermacromolecular interactions are very important in natural biological systems [1-3] as well as in biotechnological applications [4-6]. For example, many molecules including biopolymers participate in biological functions as a molecular assembly or tissue: the self-assembly of the bacterial flagella, antigen-antibody reactions, the high activity and selectivity of enzymes, etc., is accurately achieved by intermacromolecular interactions [1]. The binding of proteins to nucleic acids, which are natural polyelectrolyte, is an integral step in gene regulation [1, 7, and 8]. A weak intermacromolecular interactions are responsible for a dramatically changes in thermodynamic compatibility of biopolymers [9-11]. Intermacromolecular interactions can be utilized for isolation of proteins [4, 5, and 12] and enzymes [13], enzyme immobilization [3, 14], encapsulation [15] and drug delivery [14, 16]. The most intriguing type of complexes is that containing two proteins [1]. When two or more protein binds together, often to carry out their biological function [2]. Proteins might interact for a long time to form part of a protein complex, [17] or a protein may interact briefly with another protein just to modify it [18]. Therefore understanding of the effect of protein structure on protein-protein interactions, for example, of smooth and skeletal muscle proteins permit the manipulation of protein side chains in order to enhance gelation properties. Of particular interest would be studies on the mechanism of complexation as well as on the molecular characteristic of resulting complexes. These studies have also aided in the understanding of biological systems. This application note highlights the use of the Malvern Zetasizer Nano ZS for characterization of interbiopolymer complexes [19]. However, data are lacking for understanding of how structural and aggregation properties of the interacting proteins affect structure formation, of complexes.
