Quantifying Intermolecular Interactions

Atomic force microscopes can generate a highly detailed topological map of a specimen by moving a stylus coupled to a cantilever over the sample surface, using a laser to measure deflection of the cantilever.1 Now, researchers at the University of California at Berkeley have adopted this principle to create a system capable of quantifying intermolecular interactions, with potential applications for both clinicians and high-throughput proteomics researchers.2 In a research article published in

Written byJeffrey Perkel
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In a research article published in the September issue of Nature Biotechnology, Arun Majumdar, professor of mechanical engineering at Berkeley, and coauthors at Oak Ridge National Laboratory in Oak Ridge, Tenn., the University of Southern California in Los Angeles, and the Lawrence Berkeley National Laboratory at UC-Berkeley, describe a system to quantify prostate-specific antigen (PSA), a prostate cancer protein marker.

The PSA test uses a cantilever 200 mm long and 0.5 mm wide, one side of which is coated with gold and conjugated to an antibody that recognizes PSA. Majumdar and his colleagues incubated the cantilever, which is a diving board-like device, with a simulated human serum that contained high concentrations of human plasminogen, human serum albumin, or bovine serum albumin, with varying concentrations of PSA. When the antibodies on the cantilever captured the PSA in the solution, the device bent a few nanometers in height. A laser beam aimed ...

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