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LabAutomation 2006 - SLAS

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<strong>LabAutomation</strong><strong>2006</strong><br />

4:30 pm Monday, January 23, <strong>2006</strong> Track 1: Detection & Separation Room: Catalina<br />

Wyndham Palm Springs Hotel<br />

Claude Dufresne<br />

Co-Author(s)<br />

Merck Research Laboratories<br />

Chris Napolitano<br />

Rahway, New Jersey<br />

Sal Siciliano<br />

c_dufresne@merck.com<br />

Jesus Martin<br />

Scott Feighner<br />

Don Conway<br />

Neal Simpson<br />

Gary Kath<br />

The implementation of Remp Tube Storage Technology in support of Lead<br />

Optimization Processes.<br />

Over the past decade, many improvements have been made in automating and operating high throughput screening facilities, in the ‘hit<br />

discovery’ phase of the drug discovery process. In comparison, relatively less attention has been paid to its downstream cousin, the ‘lead<br />

optimization’ phase. As part of a larger initiative to apply intelligent industrialization to a greater number of processes, we have setup a<br />

Facility for Automation and Screening Technology (‘FAST’) dedicated to supporting processes at the interface of medicinal chemistry and<br />

biology laboratories.<br />

Part of this operation consists of storing samples from active chemistry programs for rapid turnaround in order to provide assay-ready<br />

plates to various therapeutic area biology groups. We selected the concept of multi-access tube racks as the basis of this storage. We<br />

then implemented it using a REMP Small Size Store (SSS) which integrates a Tube Punching Module to handle the capped mini-tubes.<br />

For the final integration into our liquid handling systems, we designed a custom automation instrument that integrates a REMP 8 channel<br />

manual decapper with a REMP 2D Reatrix Barcode reader. This poster will describe how the technology is integrated and used.<br />

10:30 am Tuesday, January 24, <strong>2006</strong> Track 1: Detection & Separation Room: Catalina<br />

Wyndham Palm Springs Hotel<br />

Terry D. Lee<br />

Co-Author(s)<br />

Beckman Research Institute of the City of Hope<br />

Jason Shih, Jun Xie, California Institute of Technology<br />

Duarte, California<br />

tdlee@coh.org<br />

Yunan Miao, Beckman Research Institute of the City of Hope<br />

Yu-Chong Tai, California Institute of Technology<br />

Chip Based Liquid Chromatography Systems<br />

In recent years, there has been considerable research devoted to the development of microfluidic platforms capable of performing<br />

small-scale separations. Nearly every type of electrophoretic or electrokinetic driven separation has been demonstrated in a chip-based<br />

platform including: capillary electrophoresis (CE), isoelectric focusing (IEF), micellar electrokinetic chromatography (MEKC), and capillary<br />

electrochemical chromatography (CEC). This reflects a strong preference among researchers in the field for approaches where processes<br />

can be controlled simply by adjusting voltage potentials at different points in the microfluidic system. Despite this considerable advantage<br />

and the progress that has been made, there are a number of drawbacks, including the need to work with very high voltages; a strong<br />

dependence of performance on the nature of the solvent system; limits to the range of sample types that can be analyzed; and difficulties<br />

with interfacing to MS. LC is still the method of choice for many applications including many analytical methods in the field of proteomics.<br />

Some progress has been made towards performing HPLC separations in chip-based platforms, but in most instances, a conventional<br />

LC pumping system is used to provide the pressurized flow. We now report the fabrication of a chip based LC system where all of the<br />

components including sample and solvent pumps, gradient mixer, reverse phase column, and electrospray source are contained on a single<br />

chip. Key to the design is the use of an electrochemical pumping system capable of providing the high pressures required for adequate<br />

LC separations. When interfaced to an ion trap mass spectrometer, the system is capable of performing LC-MS/MS analyses of complex<br />

peptide mixtures, with results comparable to those obtained with state-of-the-art commercial systems. This presentation will also include<br />

discussion of issues related to accurate flow control and gradient formation, and the interface to MALDI mass spectrometry.<br />

54

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