omation mbers - Society for Laboratory Automation and Screening

5:00 pm Wednesday, February 4 Genomics – Informatics Room A1
Dave Riling
DataCentric Automation
2525 Perimeter Place Drive, Suite 131
Nashville, Tennessee 37214
dave.riling@dcacorp.com
The Changing Face of Lab Automation
103
Co-Author(s)
Greg Nordstrom
DataCentric Automation
Onkar Singh
GlaxoSmithKline
As technology evolves, automation equipment becomes more and more capable and flexible. With this growing
wealth of capability the demand by the scientist to conduct experiments faster, easier, and with higher reliability
is also growing. This duality is creating a new paradigm in laboratory automation, “Solution Based Systems”.
The traditional laboratory piece wise robotics with a non-coupled LIMS environment is rapidly being replaced
with systems designed to incorporate various pieces of equipment to solve specific problems such as High
Throughput Screen Systems or Automated Protein Crystallization Systems, but this merely marks the beginning
of a broader shift in laboratory automation trends. Innovations in lab automation systems continue at a rapid
rate thus today’s state of art is tomorrow’s closet junk. In order to break this cycle and provide workable cost
effective solutions for the drug discovery arena a radical approach is emerging, Highly Adaptive Integrated Solution
Environments which strongly couple the ease of experiment modification with comprehensive data collection and
analysis methods to integrated lab automation solution based systems. This talk will focus on this emerging trend,
discuss the advantages of this new environment for both scientist and engineer, and describe how to get your lab
ready to push the envelope without large upfront costs or long-term paralysis in selecting new and replacement
equipment. This talk will conclude with a discussion on how this new trend will benefit the scientist through
automated optimization algorithms which are described in an actual implementation of a hybrid Automated Protein
Crystallization System.
8:00 am Thursday, February 5 Genomics – Arrays Room A1
J. Colin Cox
University of Texas
1 University Station, A4800
Austin, Texas 78712-0159
j.colin.cox@mail.utexas.edu
Co-Author(s)
Travis S. Bayer
Jim Collett
Andrew D. Ellington
Automated Aptamer Selection: Applications in RNA: Protein Sequence Specificity, and
Aptamer-chip Microarrays
In vitro selection and evolution is incredibly adept at producing nucleic acid binding species (aptamers). Like
antibodies, these nucleic acid aptamers typically interact with their ligands with exceptionally high specificity and
affinity. Their potential utility become even more evident when one considers the astonishingly large range of target
ligands. Aptamers have been generated to bind ligands ranging from small ions to rat tails. Nucleic acid species
can be manually evolved in significantly less time than required for antibody production. Regardless, typical
selections can take upwards of weeks to a few months to finish. Our laboratory has pioneered the process of
automating in vitro selection, facilitating the creation of aptamers in mere days. This ability bodes well for the rapid
development of both large-scale aptamer-based evolutionary specificity studies as well as nucleic acid-based
biosensor arrays. Presented herein are examples of these two branches of aptamer employment. Aptamers are
uniquely suited for determining sequence recognition motifs of nucleic-acid binding proteins. We have explored the
natural diversity of RNA binding peptides and proteins by investigating arginine-rich RNA binding motifs (ARMs)
from eukaryotes, prokaryotes, and viruses that infect both. In addition, we have engineered several mutations
of the human spliceosomal U1A protein and evolved aptamers to each mutant in order to elucidate nucleic-acid
sequence:protein sequence binding “rules”. Finally, we have created novel aptamer-array chips that function
similarly to traditional DNA-array chips. Aptamers on chips bind ligands as they would in solution, and these
biosensing chips allow for the parallel measurement of multiple aptamer-ligand binding investigations.
PODIUM ABSTRACTS