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omation mbers - Society for Laboratory Automation and Screening

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TP064<br />

Dominik Poetz<br />

National Institute of St<strong>and</strong>ards <strong>and</strong> Technology<br />

Analytical Chemistry Division<br />

100 Bureau Drive<br />

Gaithersburg, Maryl<strong>and</strong> 20899<br />

dominik.poetz@nist.gov<br />

Using the Analytical In<strong>for</strong>mation Markup Language (AnIML) to Represent LC-Diode-Array<br />

Data<br />

ASTM Subcommittee E13.15 has been <strong>for</strong>med, in part, to develop a st<strong>and</strong>ard markup language <strong>for</strong> spectroscopic<br />

<strong>and</strong> chromatographic result data. The Analytical In<strong>for</strong>mation Markup Language (AnIML) is being created using the<br />

Extensible Markup Language (XML) <strong>and</strong> is based on existing markup languages <strong>for</strong> analytical result data such as<br />

NIST’s SpectroML <strong>and</strong> Thermo’s GAML as well as data definitions <strong>and</strong> concepts from existing st<strong>and</strong>ards such as<br />

JCAMP-DX, the ASTM’s Andi st<strong>and</strong>ards, IUPAC definitions, etc. The initial work has begun to create the AnIML<br />

core, the schema representing the data <strong>and</strong> metadata common to all analytical spectroscopy <strong>and</strong> chromatography<br />

techniques. The E13.15 subcommittee has asked NIST to develop an example implementation of AnIML <strong>for</strong> data<br />

from liquid chromatography with diode array detection. This technique was chosen as a model because it is not<br />

overly complex, as contrasted with mass spectrometry or nuclear magnetic resonance spectroscopy, <strong>and</strong> because<br />

the datasets are inherently two-dimensional. The implementation will be created around the AnIML core <strong>and</strong> will<br />

consist of a “technique-specific” layer <strong>for</strong> LC-diode arrays that is vendor independent, along with enough of a<br />

“vendor-specific” layer to realize the application <strong>for</strong> at least one existing commercial instrument. The goal is to<br />

create a sufficient AnIML representation <strong>for</strong> data from a actual analytical technqiue to see what works <strong>and</strong> what<br />

needs revision, to demonstrate the power of the markup language approach, <strong>and</strong> to serve as a model <strong>for</strong> those<br />

writing technique specific layers <strong>for</strong> other analytical spectroscopy <strong>and</strong> chromatography domains.<br />

TP065<br />

Ketul C. Popat<br />

Boston University<br />

Department of Biomedical Engineering<br />

44 Cummington Street<br />

Boston, Massachusetts 02215<br />

kpopat@bu.edu<br />

178<br />

Co-Author(s)<br />

Tejal A. Desai <strong>and</strong> Gopal Mor, Boston University<br />

Craig Grimes, Pennsylvania State University<br />

Poly-Ethylene-Glycol Grafted Non-fouling Nanoporous Alumina Membranes<br />

Membranes currently used <strong>for</strong> separation of sub-micron particles in biomedical applications are of asymmetric<br />

or anisotropic variety <strong>and</strong> are made from polymers such as polysulfone or polyacrylonitrile. Several<br />

bioincompatibilities are associated with these polymeric membranes limiting their applications. Aluminum oxide<br />

substrates have been chosen <strong>for</strong> several reasons, including compatibility with our processing protocols, chemical<br />

<strong>and</strong> thermal stability, <strong>and</strong> ease in post-processing surface modification. Several studies have shown this material<br />

to be bioinert. However, the biocompatibility of the membrane material must be further investigated <strong>and</strong> improved.<br />

With proper surface modification, the protein adsorption can be lowered <strong>and</strong> the non-fouling characteristics can<br />

be improved. In this study we graft alumina membranes with a biocompatible polymer like poly (ethylene glycol) to<br />

investigate protein adsorption. Albumin <strong>and</strong> Fibrinogen were selected as model proteins since they are important<br />

components in immunogenic <strong>and</strong> thrombogenic reactions. X-ray photoelectron spectroscopy (XPS) <strong>and</strong> atomic<br />

<strong>for</strong>ce microscopy (AFM) were used to characterize PEG films on alumina membranes.

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