Polymer complexes were formed through electrostatic interaction in poly(methacry1ic acid)-integral type polycation systems and hydrogen bonding in the poly(methacry1ic acid)-poly(N-vinyl-2-pyrrolidone) system in several solvents. The composition of the polyelectrolyte complex was affected by the chemical properties of solvents, e.g., the dissociation of the component polyelectrolyte was interferred with decreasing the polarity of the solvent. The heats of mixing in case of the combination of poly(methacry1ic acid)-poly(N-vinyl-2-pyrrolidone) were negative in N,N-dimethylformamide but they were positive in water. In polyelectrolyte complex systems, they could not be measured by reason of some experimental difficulties. These results indicate that solvation of the component polymers is very important to clarify the mechanism of the formation of polymer complexes.
A pair of polymers may interact with each other through hydrogen bond and form a polymer complex. Such polymer complex formation is affected by several chemical and physical factors, especially by solvent properties. This solvent effect was studied in the complex formation of poly(methacry1ic acid) with a series of proton-accepting polymers in aprotic solvents. The extraordinary behaviour of polymer complexes in dimethyl sulfoxide was well explained in terms of the strong interaction between proton-donating polymer and dimethyl sulfoxide. In addition, a stronger proton-accepting polymer, viz. poly(N,N-dimethyl-N',N',N",N"-tetramethylenephosphoramide), was synthesized. This polymer could form a polymer complex with poly(methacry1ic acid) through hydrogen bond even in dimethyl sulfoxide. Selective polymer complex formation was achieved by controlling such solvent properties.
The interactions of human serum proteins with synthetic macromolecules were studied in heterogeneous solution systems. An alternating copolymer of styrene with maleic anhydride was crosslinked by diamines with different number of methylene groups varying from 2 to 10, and the degree of crosslinking (mole fraction of amide linked units) was changed from 7 to 43% in order to elucidate the effects of pore size, density of ionic site, and flexibility of the macromolecules. The adsorption of serum proteins on the resins was studied with human serum albumin and y-globulin as typical proteins in human serum. The resins were dispersed in phosphate buffer solutions, and these were mixed with the phosphate buffer solutions of albumin and/or y-globulin. After a suitable period of incubation at 20 "C, the mixed solutions were centrifuged. The degree of protein-adsorption was determined from the remaining amounts of proteins in the supernatant as measured by U.V. spectrometry. It was observed that the adsorption of albumin was influenced by the subtle balance of hydrophobicity and hydrophilicity of the resin. On the other hand, y-globulin was adsorbed not only by the hydrophobic resin but also by the hydrophilic (ionic) resin. The resin which was crosslinked to 16% by hexamethylenediamine showed high affinity towards y-globulin at pH 7,4. Selective adsorption was also possible: Almost all of the y-globulin and only little of the albumin were adsorbed within half an hour at 20°C by the use of this resin.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.