10.1007/s11176-008-1024-z

Abstract

Complex formation of scleroprotein models with an N-methylmorpholine N-oxide solvent was studied by the semiempirical PM3 method.Scleroproteins include a large group of fibrous proteins abundant in animal tissues: silk fibroin, fur and feather keratins, connective tissue collagen and elastin, and marine sponge and coral spongin. Since these proteins are fiber and film-forming, interest in their reprocessing by dissolution with the aim to obtain various items for medicine and biotechnology is constantly growing [135]. Search for new solvents and processing technologies for these natural polymers with unique properties is impossible without understanding of their structural features and mechanism of dissolution. Modern methods of computer simulation play special role in studying dissolution processes. Their results help to explain experimentally obtained regularities and predict the behavior of polymers upon dissolution. The aim of this work was to study the mechanism of dissolution of models of scleroprotein crystal structure by a quantumchemical method.