earticle

영어

Recent progress in polymer nanotechnology has been directed to the application of biodegradable nanoassemblies based on natural proteins and polysaccharides as drug delivery systems, due to their biodegradation, sustained-release properties, sub-cellular size and stability. Recombinant human gelatin-based nanoparticles were prepared by a simple coacervation method, which are suitable for the hydrophilic protein drug delivery. In addition,
a hydrophobically modified glycol chitosan (HGC) was prepared by a conjugation of glycol chitosan with 5β-cholanic acid. In aqueous phases, the HGC conjugates formed nanoparticles. Their hydrophobic cores were surrounded with a hydrophilic outer domain. The inner domain can serve as a nano-reservoir for a variety of hydrophobic anticancer drugs. The characteristics
of nanoparticles were investigated by various physicochemical techniques to examine the possibility as drug carriers. Although recent progress in biotechnology enables production of various protein drugs for therapeutic purposes, several challenges still remain, including enzymatic susceptibility, stability during storage, and efficacy after administration into the body.
Promising approaches to overcome these limitations is to use nanoparticular drug delivery systems or in situ forming gels to achieve the controlled protein drug release, systemically or locally, over a long period of time. The controlled local drug delivery is aimed to facilitate high site-specific concentrations of therapeutic agents with prolonged retention at lower doses with reduced systemic toxicity. In situ gels can solve the problems associated with most widely used biodegradable microsphere formulations, such as the drug loss caused by low encapsulation efficiencies of microspheres, the use of harsh organic solvent and manufacturing costs increases by several processes.
Definitely, the parenteral delivery including in-situ polymer gels is currently most demanding and suitable for the successful development of recombinant therapeutic proteins by stabilizing and controlling the release rate of sensitive proteins.