Abstract
Recently, the polyion complex (PIC) micelle has been suggested as a promising carrier system for peptide and proteins. However, its utilities are limited by its sensitivity to the environment such as dilution and ionic strength of the solution. In this study, to overcome these obstructions, PIC micelles prepared from an anionic block copolymer, poly(ethylene glycol)-poly(alpha,beta-aspartic acid), and a cationic protein, trypsin, were cross-linked with glutaraldehyde through the Schiff base formation. On the basis of a light scattering technique, the results revealed an efficient resistance of the cross-linked PIC micelle to a high salt concentration, which was a key parameter controlling the structure of the PIC micelles. Moreover, the stability of trypsin after cross-linking was remarkably improved. Evidently, as a bionanoreactor and/or bionanoreservoir, the PIC micelles entrapping protein molecules in the cross-linked core reveal an improved stability, allowing their wide application in the fields of biotechnology and pharmaceutical sciences.
Published Version
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