Journal
BIOPHYSICAL CHEMISTRY
Volume 275, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bpc.2021.106605
Keywords
gamma-polyglutamic acid; Chitosan; Chemical stabilization; Protein folding; pH depending structure
Funding
- Iran's National Elites Foundation
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The study found that grafting chitosan onto gamma-polyglutamic acid can effectively inhibit the formation of protein aggregates; the stability of CS-g-PGA is strongly dependent on pH, as revealed through the evaluation of various stabilizers; Chitosan under optimized conditions may serve as an important precursor for the pharmaceutical industry and function as a new polymer for aggregation suppression and protein stabilization.
In protein-based formulations, conformational distortions and attractive interactions may cause insoluble and undesired aggregates. In the case of ionic peptides, including cationic or anionic, commonly electrostatic interactions are the main factors that control structure assembling. In this study, it was proposed that grafting of chitosan (CS) to gamma-polyglutamic acid (gamma-PGA) might exhibit much strong inhibiting effect on the formation of protein aggregates due to multiple amino groups and hydrophilic properties. To guarantee stable and safe biopharmaceutical formulation, the potency of a variety of stabilizers including sugars (glucose, sucrose), polyols (sorbitol, glycerol), surfactant (Tween 20), salting-out salt (PBS), and also different pH values have been evaluated on stabilizing or destabilizing the native state of CS-g-PGA copolymer using FTIR, CD, DLS, and SDS-PAGE. The comparable analysis revealed that the stability of CS-g-PGA was strongly dependent on pH owing to the polyelectrolyte characteristics of the polymers. Altogether these results implied that CS at optimized conditions might be an important precursor for the pharmaceutical industry and function as a new polymer for aggregation suppression and protein stabilization.
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