Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 128, Issue 8, Pages 2635-2640Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja0555668
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Funding
- NIAID NIH HHS [AI21144] Funding Source: Medline
- NIGMS NIH HHS [GM63025] Funding Source: Medline
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A general method of rigid, specific labeling of proteins with gold clusters has been devised. The method relies on the conjugation of a glutathione monolayer-protected gold cluster (MPC) with a single chain Fv antibody fragment (scFv), mutated to present an exposed cysteine residue. Efficient formation of a gold-thiolate bond between the MPC and scFv depends on activation of the gold cluster by chemical oxidation. Once formed, the MPC-scFv conjugate is treated with a reductant to quench cluster reactivity. The procedure has been performed with an MPC with an average Au-71 core and an scFv directed against a tetrameric protein, the influenza neuraminidase. A complex of the MPC-scFv conjugate with the neuraminidase was isolated, and the presence of four gold clusters was verified by cryoelectron microscopy.
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