Combining MALDI FTMS, comparative glycoproteomics, and bioinformatics for the discovery of biomarkers in Prion disease

ANYL 317

Lingjun Li, lli@pharmacy.wisc.edu1, Xin Wei2, Joshua Schmidt1, Allen Herbst3, Sean McIlwain4, David Page4, and Judd Aiken3. (1) School of Pharmacy & Department of Chemistry, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI 53705, (2) Department of Chemistry, University of Wisconsin-Madison, Madison, WI, (3) Animal Health and Biomedical Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI, (4) Department of Statistics, University of Wisconsin-Madison, Madison, WI
Prion diseases are a unique family of neurodegenerative diseases of the central nervous system that are always fatal. Clearly, there is an urgent need for the development of a reliable, sensitive, and specific ante-mortem diagnostic test for pre-clinical identification of prion-infected animals or individuals. We are developing a MS-based analytical platform in combination with a suite of bioinformatics tools to identify a panel of biomarkers in serum and cerebrospinal fluid collected from live animals infected with prion disease during the preclinical incubation period. Specifically we use high resolution MALDI Fourier transform mass spectrometry together with biostatistics to compare mass spectral profiles obtained from the body fluid samples of prion infected and control animals. Once a set of discriminating peaks is identified, sequence analysis is performed to determine their identities. Additionally, a lectin-based affinity selection coupled to isotopic formaldehyde labeling enables analysis of global glycoproteomic changes in prion disease infected animals.
 

Biomarker Discovery
1:30 PM-4:20 PM, Monday, August 20, 2007 BCEC -- 104A, Oral

Division of Analytical Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007