Abstract
A linker peptide sequence with affinity to silica-containing materials was fused to Streptococcus protein G', an antibody-binding protein. This recombinant fusion protein, linker-protein G (LPG) was produced in E. coli and exhibited strong affinity to silica-coated magnetic particles and was able to bind to them at different pHs, indicating a true pH-independent binding. LPG was used as an anchorage point for the oriented immobilization of antibodies onto the surface of the particles. These particle-bound "LPG-Antibody complexes" mediated the binding and recovery of different cell types (e.g., human stem cells, Legionella, Cryptosporidium and Giardia), enabling their rapid and simple visualization and identification. This strategy was used also for the efficient capture of Cryptosporidium oocysts from water samples. These results demonstrate that LPG can mediate the direct biofunctionalization of silica-coated magnetic particles without the need for complex surface chemical modification.
| Language | English |
|---|---|
| Article number | 2543 |
| Pages | 1-9 |
| Number of pages | 9 |
| Journal | Journal of Nanoparticle Research |
| Volume | 16 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 2014 |
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Biofunctionalization of silica-coated magnetic particles mediated by a peptide. / Care, Andrew; Chi, Fei; Bergquist, Peter L.; Sunna, Anwar.
In: Journal of Nanoparticle Research, Vol. 16, No. 8, 2543, 2014, p. 1-9.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Biofunctionalization of silica-coated magnetic particles mediated by a peptide
AU - Care, Andrew
AU - Chi, Fei
AU - Bergquist, Peter L.
AU - Sunna, Anwar
PY - 2014
Y1 - 2014
N2 - A linker peptide sequence with affinity to silica-containing materials was fused to Streptococcus protein G', an antibody-binding protein. This recombinant fusion protein, linker-protein G (LPG) was produced in E. coli and exhibited strong affinity to silica-coated magnetic particles and was able to bind to them at different pHs, indicating a true pH-independent binding. LPG was used as an anchorage point for the oriented immobilization of antibodies onto the surface of the particles. These particle-bound "LPG-Antibody complexes" mediated the binding and recovery of different cell types (e.g., human stem cells, Legionella, Cryptosporidium and Giardia), enabling their rapid and simple visualization and identification. This strategy was used also for the efficient capture of Cryptosporidium oocysts from water samples. These results demonstrate that LPG can mediate the direct biofunctionalization of silica-coated magnetic particles without the need for complex surface chemical modification.
AB - A linker peptide sequence with affinity to silica-containing materials was fused to Streptococcus protein G', an antibody-binding protein. This recombinant fusion protein, linker-protein G (LPG) was produced in E. coli and exhibited strong affinity to silica-coated magnetic particles and was able to bind to them at different pHs, indicating a true pH-independent binding. LPG was used as an anchorage point for the oriented immobilization of antibodies onto the surface of the particles. These particle-bound "LPG-Antibody complexes" mediated the binding and recovery of different cell types (e.g., human stem cells, Legionella, Cryptosporidium and Giardia), enabling their rapid and simple visualization and identification. This strategy was used also for the efficient capture of Cryptosporidium oocysts from water samples. These results demonstrate that LPG can mediate the direct biofunctionalization of silica-coated magnetic particles without the need for complex surface chemical modification.
UR - http://www.scopus.com/inward/record.url?scp=84904275943&partnerID=8YFLogxK
U2 - 10.1007/s11051-014-2543-7
DO - 10.1007/s11051-014-2543-7
M3 - Article
VL - 16
SP - 1
EP - 9
JO - Journal of Nanoparticle Research
T2 - Journal of Nanoparticle Research
JF - Journal of Nanoparticle Research
SN - 1388-0764
IS - 8
M1 - 2543
ER -