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In JoVE (1)
- Het analyseren van cellulaire internalisatie van nanodeeltjes en bacteriën door Multi-spectrale Imaging flowcytometrie
Other Publications (1)
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Articles by Gregory J. Phillips in JoVE
Het analyseren van cellulaire internalisatie van nanodeeltjes en bacteriën door Multi-spectrale Imaging flowcytometrie
Yashdeep Phanse1, Amanda E. Ramer-Tait1, Sherree L. Friend2, Brenda Carrillo-Conde3, Paul Lueth1, Carrie J. Oster1, Gregory J. Phillips1, Balaji Narasimhan3, Michael J. Wannemuehler1, Bryan H. Bellaire1
1Department of Veterinary Microbiology and Preventive Medicine, Iowa State University, 2Amnis Corporation, 3Department of Chemical and Biological Engineering, Iowa State University
In dit artikel beschrijven we een methode gebruik te maken van multi-spectraal imaging flowcytometrie om de internalisering van polyanhydride nanodeeltjes of bacteriën door RAW 264.7 cellen te kwantificeren.
Other articles by Gregory J. Phillips on PubMed
Acta Biomaterialia. Aug, 2010 | Pubmed ID: 20123135
The design of biodegradable polymeric delivery systems based on polyanhydrides that would provide for improved structural integrity of Yersinia pestis antigens was the main goal of this study. Accordingly, the full-length Y. pestis fusion protein (F1-V) or a recombinant Y. pestis fusion protein (F1(B2T1)-V10) was encapsulated and released from microparticles based on 1,6-bis(p-carboxyphenoxy)hexane (CPH) and sebacic acid (SA) copolymers and 1,8-bis(p-carboxyphenoxy)-3,6-dioxaoctane (CPTEG) and CPH copolymers fabricated by cryogenic atomization. An enzyme-linked immunosorbent assay was used to measure changes in the antigenicity of the released proteins. The recombinant F1(B2T1)-V10 was unstable upon release from the hydrophobic CPH:SA microparticles, but maintained its structure and antigenicity in the amphiphilic CPTEG:CPH system. The full-length F1-V was stably released by both CPH:SA and CPTEG:CPH microparticles. In order to determine the effect of the anhydride monomers on the protein structure, changes in the primary, secondary, and tertiary structure, as well as the antigenicity of both Y. pestis antigens, were measured after incubation in the presence of saturated solutions of SA, CPH, and CPTEG anhydride monomers. The results indicated that the amphiphilic environment provided by the CPTEG monomer was important to preserve the structure and antigenicity of both proteins. These studies offer an approach by which a thorough understanding of the mechanisms governing antigenic instability can be elucidated in order to optimize the in vivo performance of biodegradable delivery devices as protein carriers and/or vaccine adjuvants.