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Rendering protein-based particles transiently insoluble for therapeutic applications.


ABSTRACT: Herein, we report the fabrication of protein (bovine serum albumin, BSA) particles which were rendered transiently insoluble using a novel, reductively labile disulfide-based cross-linker. After being cross-linked, the protein particles retain their integrity in aqueous solution and dissolve preferentially under a reducing environment. Our data demonstrates that cleavage of the cross-linker leaves no chemical residue on the reactive amino group. Delivery of a self-replicating RNA was achieved via the transiently insoluble PRINT protein particles. These protein particles can provide new opportunities for drug and gene delivery.

SUBMITTER: Xu J 

PROVIDER: S-EPMC3365610 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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Rendering protein-based particles transiently insoluble for therapeutic applications.

Xu Jing J   Wang Jin J   Luft J Christopher JC   Tian Shaomin S   Owens Gary G   Pandya Ashish A AA   Berglund Peter P   Pohlhaus Patrick P   Maynor Benjamin W BW   Smith Jonathan J   Hubby Bolyn B   Napier Mary E ME   DeSimone Joseph M JM  

Journal of the American Chemical Society 20120517 21


Herein, we report the fabrication of protein (bovine serum albumin, BSA) particles which were rendered transiently insoluble using a novel, reductively labile disulfide-based cross-linker. After being cross-linked, the protein particles retain their integrity in aqueous solution and dissolve preferentially under a reducing environment. Our data demonstrates that cleavage of the cross-linker leaves no chemical residue on the reactive amino group. Delivery of a self-replicating RNA was achieved vi  ...[more]

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