X-ray crystal structure of an anti-Buckminsterfullerene antibody fab fragment: biomolecular recognition of C(60).
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.
Braden
B C
BC
Department of Natural Sciences, Bowie State University, Bowie, MD 20715, USA. bbraden@bowiestate.edu
Goldbaum
F A
FA
Chen
B X
BX
Kirschner
A N
AN
Wilson
S R
SR
Erlanger
B F
BF
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002244:Carbon / Q000276:immunology*; D018360:Crystallography, X-Ray; D037741:Fullerenes; D006825:Hybridomas; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry*; D051379:Mice; D008807:Mice, Inbred BALB C; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D037741:Fullerenes; D007140:Immunoglobulin Fab Fragments; D002244:Carbon; C069837:fullerene C60