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Controlled-release and preserved bioactivity of proteins from (self-assembled) core-shell double-walled microspheres

Authors Yuan W, Liu Z

Received 25 October 2011

Accepted for publication 13 November 2011

Published 13 January 2012 Volume 2012:7 Pages 257—270

DOI https://doi.org/10.2147/IJN.S27621

Review by Single-blind

Peer reviewer comments 2


This paper has been retracted
 
Weien Yuan1,2, Zhenguo Liu1

1Department of Neurology, Xinhua Hospital, affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, 2School of Pharmacy, Shanghai Jiao Tong University, Shanghai, People’s Republic of China

Abstract: In order to address preserved protein bioactivities and protein sustained-release problems, a method for preparing double-walled microspheres with a core (protein-loaded nanoparticles with a polymer-suspended granule system-formed core) and a second shell (a polymer-formed shell) for controlled drug release and preserved protein bioactivities has been developed using (solid-in-oil phase-in-hydrophilic oil-in-water (S/O/Oh/W)) phases. The method, based on our previous microsphere preparation method (solid-in-oil phase-in-hydrophilic oil-in-water (S/O/Oh/W), employs different concentric poly(D,L-lactide-co-glycolide), poly(D,L-lactide), and protein-loaded nanoparticles to produce a suspended liquid which then self-assembles to form shell-core microspheres in the hydrophilic oil phase, which are then solidified in the water phase. Variations in the preparation parameters allowed complete encapsulation by the shell phase, including the efficient formation of a poly(D,L-lactide) shell encapsulating a protein-loaded nanoparticle-based poly(D,L-lactide-co-glycolide) core. This method produces core-shell double-walled microspheres that show controlled protein release and preserved protein bioactivities for 60 days. Based upon these results, we concluded that the core-shell double-walled microspheres might be applied for tissue engineering and therapy for chronic diseases, etc.

Keywords: protein delivery, protein stability, core-shell microspheres, dextran nanoparticles

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