Background: Con A, a lectin extract from jackbean Canavalia ensiformis is known for
its agglutination activity. ZnO nanoparticles promote the faster electron transfer between the lectin
immobilized and the target cells. Hence, Con A immobilized on ZnO nanoparticles will agglutinate
cells more effectively than the native protein.
Objectives: Concanavalin A (Con A), a lectin was immobilized on the hexagonal zinc oxide (ZnO)
nanoparticles to monitor its activity on RBCs and lymphocytes.
Methods: The immobilization of Con A and zinc oxide nanoparticles has been studied by molecular
docking, microscopic and genotoxicity assessment techniques.
Results: Qualitative assessment using various techniques like atomic force microscopy, scanning
electron microscopy and X-ray diffraction showed minor changes in morphology of Con A and
ZnO nanoparticles. FT-IR spectroscopy confirmed the linking of Con A amino groups with ZnO
nanoparticles. Con A immobilized nanoparticles in contrast to native lectin showed minor changes
in hemagglutination activity as confirmed by pH dependence studies using fluorimetry. Con Aimmobilized
nanoparticles retained the agglutination activity, this can be indicative of their potential
application in detection of virus transformed and neoplastic cells. The Con A immobilized ZnO
nanoparticles did not induce any significant but minor damage to whole cell DNA as revealed from
comet assay or plasmid DNA.
Conclusion: Con A immobilized on ZnO nanoparticles showed minor changes in the structure of
ZnO nanoparticles and in the conformational of native Con A. However, Con A immobilized ZnO
nanoparticles interestingly, showed pH resistance and better hemagglutination activity as well as
minor DNA damage to whole cell lymphocytes. Thus, this novel bioaffinity support has prospective