X-ray crystal structure of an anti-Buckminsterfullerene antibody fab fragment: biomolecular recognition of C(60).

Braden BC, Goldbaum FA, Chen BX, Kirschner AN, Wilson SR, Erlanger BF
Proc Natl Acad Sci U S A. 2000 97 (22): 12193-7

PMID: 11035793 · PMCID: PMC17317 · DOI:10.1073/pnas.210396197

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.

MeSH Terms (13)

Amino Acid Sequence Animals Antibodies, Monoclonal Carbon Crystallography, X-Ray Fullerenes Hybridomas Immunoglobulin Fab Fragments Mice Mice, Inbred BALB C Models, Molecular Molecular Sequence Data Protein Conformation

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