X-ray crystal structure of an anti-Buckminsterfullerene antibody Fab fragment: Biomolecular recognition of C60
BC Braden, FA Goldbaum, BX Chen… - Proceedings of the …, 2000 - National Acad Sciences
BC Braden, FA Goldbaum, BX Chen, AN Kirschner, SR Wilson, BF Erlanger
Proceedings of the National Academy of Sciences, 2000•National Acad SciencesWe have prepared a monoclonal Buckminsterfullerene specific antibody and report the
sequences of its light and heavy chains. We also show, by x-ray crystallographic analysis of
the Fab fragment and by model building, that the fullerene binding site is formed by the
interface of the antibody light and heavy chains. Shape-complementary clustering of
hydrophobic amino acids, several of which participate in putative stacking interactions with
fullerene, form the binding site. Moreover, an induced fit mechanism appears to participate …
sequences of its light and heavy chains. We also show, by x-ray crystallographic analysis of
the Fab fragment and by model building, that the fullerene binding site is formed by the
interface of the antibody light and heavy chains. Shape-complementary clustering of
hydrophobic amino acids, several of which participate in putative stacking interactions with
fullerene, form the binding site. Moreover, an induced fit mechanism appears to participate …
We have prepared a monoclonal Buckminsterfullerene specific antibody and report the sequences of its light and heavy chains. We also show, by x-ray crystallographic analysis of the Fab fragment and by model building, that the fullerene binding site is formed by the interface of the antibody light and heavy chains. Shape-complementary clustering of hydrophobic amino acids, several of which participate in putative stacking interactions with fullerene, form the binding site. Moreover, an induced fit mechanism appears to participate in the fullerene binding process. Affinity of the antibody–fullerene complex is 22 nM as measured by competitive binding. These findings should be applicable not only to the use of antibodies to assay and direct potential fullerene-based drug design but could also lead to new methodologies for the production of fullerene derivatives and nanotubes as well.
National Acad Sciences