Biofunctionalization of silica-coated magnetic particles mediated by a peptide

Andrew Care, Fei Chi, Peter L. Bergquist, Anwar Sunna*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


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.

Original languageEnglish
Article number2543
Pages (from-to)1-9
Number of pages9
JournalJournal of Nanoparticle Research
Issue number8
Publication statusPublished - 2014


  • Biofunctionalization
  • Biomedicine
  • Cell capture
  • Nanoparticles
  • Peptide-mediated binding


Dive into the research topics of 'Biofunctionalization of silica-coated magnetic particles mediated by a peptide'. Together they form a unique fingerprint.

Cite this