omation mbers - Society for Laboratory Automation and Screening
omation mbers - Society for Laboratory Automation and Screening
omation mbers - Society for Laboratory Automation and Screening
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4:30 pm Wednesday, February 4 HT Chemistry – New Strategies Room B3<br />
Jonathan Ellman<br />
University of Cali<strong>for</strong>nia, Berkeley<br />
826 Latimer Hall<br />
Berkeley, Cali<strong>for</strong>nia 94720-1460<br />
jellman@uclink.berkeley.edu<br />
New Approaches <strong>for</strong> High Throughput Heterocycle Synthesis<br />
The first approach is based upon enantiomerically pure tert-butanesulfinamide, which has been developed in my<br />
laboratories. This chiral amine reagent is now employed extensively in the pharmaceutical industry. Methods will<br />
be presented <strong>for</strong> the parallel synthesis of a wide range of pharmaceutically relevant compounds from chiral amine<br />
building blocks to complex alkaloids using either solid-phase or solution-phase methods. In the second approach,<br />
C-H functionalization of organic compounds has been applied to the preparation of pharmaceutically relevant<br />
structures, including substituted indanes, tetralanes, indoles, dihydrobenzofurans, dihydroindoles, <strong>and</strong> azoles. The<br />
application of microwave chemistry to both of these approaches will also be described.<br />
5:00 pm Wednesday, February 4 HT Chemistry – New Strategies Room B3<br />
Frantisek Turecek<br />
University of Washington<br />
Bagley Hall<br />
Box 351700<br />
Seattle, Washington 98195-1700<br />
turecek@chem.washington.edu<br />
52<br />
Co-Author(s)<br />
Yuko Ogata<br />
Erkang Fan<br />
Aut<strong>omation</strong> of Bioanalytical Processes Using the Lab-on-Valve Approach. Applications to<br />
Protein Binding <strong>and</strong> Diagnosis of Inborn Errors of Metabolism<br />
A method is introduced that achieves quantitative screening of lig<strong>and</strong>s <strong>for</strong> binding with immobilized proteins.<br />
The method uses the Lab-on-Valve apparatus that is interfaced to an electrospray ionization mass spectrometer<br />
(ESI-MS), such as a quadrupole ion trap or a t<strong>and</strong>em triple quadrupole instrument. Proteins are immobilized on<br />
a solid support by covalent attachment to CNBr activated sepharose, or by non-covalent binding via biotin or<br />
His-tag conjugates to streptavidin-agarose or IMAC beads. The support with the immobilized protein is infused in<br />
the Lab-on-Valve apparatus <strong>and</strong> exposed to a mixture of potentially binding lig<strong>and</strong>s, which are eluted in a zone<br />
frontal mode. Mass spectrometric analysis is used to monitor the concentrations of the eluted components <strong>and</strong><br />
measure their breakthrough volumes. The latter are used <strong>for</strong> the calculation of binding constants <strong>for</strong> the mixture<br />
components. Examples will be given <strong>for</strong> lig<strong>and</strong> binding to cholera toxin B subunit <strong>and</strong> human peroxin PEX5.
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