X-ray crystal structure of an anti-Buckminsterfullerene antibody Fab fragment:: Biomolecular recognition of C60
X-ray crystal structure of an anti-Buckminsterfullerene antibody Fab fragment:: Biomolecular recognition of C60
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DOI：
10.1073/pnas.210396197
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发表时间：
2000-10-24
影响因子：
11.1
通讯作者：
Erlanger, BF
中科院分区：
文献类型：
--
作者：
Braden, BC;Goldbaum, FA;Erlanger, BF
我们制备了单克隆巴克敏斯特富勒烯特异性抗体并报告了其轻链和重链的序列。我们还通过 Fab 片段的 X 射线晶体学分析和模型构建表明，富勒烯结合位点是由抗体轻链和重链的界面形成的。疏水性氨基酸的形状互补簇形成了结合位点，其中一些氨基酸参与了与富勒烯的假定堆积相互作用。此外，诱导契合机制似乎参与了富勒烯结合过程。通过竞争性结合测量，抗体-富勒烯复合物的亲和力为 22 nM。这些发现不仅适用于使用抗体来分析和指导潜在的基于富勒烯的药物设计，而且还可能导致产生富勒烯衍生物和纳米管的新方法。
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.