>>FREMONT, Calif., Sept. 3 /PRNewswire-FirstCall/ -- Ciphergen Biosystems, Inc. (Nasdaq: CIPH - News) announced today that the University of Texas Medical Branch-Galveston (UTMB) and Ciphergen have received funding from the National Institute of Health (NIAID) to develop new strategies for early diagnosis of viral infections caused by exposure to bioterrorism agents.
This research project will combine UTMB's proprietary thioaptamer technology with Ciphergen's SELDI ProteinChip technology to study the inflammatory response of cytokines and key transcription factors when challenged with pathogens. In order to obtain this grant, UTMB and Ciphergen submitted preliminary data obtained from a prototype thioaptamer array. This collaboration will work towards identifying and characterizing novel protein interactions associated with viral infection, enhancing innate immunity, and controlling cytopathological immune reactions. Ultimately, this could result in protein-based diagnostics and therapeutics. The long-term objective of this collaborative effort is to develop real-time, chip-based identification and assays of host factors associated with viral infections.
William Rich, President and CEO of Ciphergen, stated, "We are delighted to be working with UTMB on this important initiative. The thioaptamer technology will allow us to rapidly develop the biochip content necessary to discover and assay the key protein players associated with pathogen challenge."
Dr. David Gorenstein, Principal Investigator at the University of Texas Medical Branch at Galveston commented, "The combination of thioaptamer technology with SELDI ProteinChip technology makes this a very exciting program."<<
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This is the only background I can find on the technology:
>>Biochemistry. 2002 Jul 30;41(30):9696-706.
Combinatorial selection and binding of phosphorothioate aptamers targeting human NF-kappa B RelA(p65) and p50.
King DJ, Bassett SE, Li X, Fennewald SA, Herzog NK, Luxon BA, Shope R, Gorenstein DG.
Department of Human Biological Chemistry and Genetics and Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 77555, USA.
Previously, we reported the in vitro combinatorial selection of phosphorothioate aptamers or "thioaptamers" targeting the transcription factor NF-IL6. Using the same approach and purified recombinant human NF-kappa B proteins RelA(p65) and p50, duplex thioaptamers have been selected that demonstrate high-affinity, competitive binding with the duplex 22-mer binding site, Ig kappa B. Binding energetics of RelA(p65) and p50 homodimers were studied using a quantitative electrophoretic mobility shift assay or EMSA. As a reference system for competitive aptamer binding, the duplex 22-mer phosphoryl binding site known as Ig kappa was determined to bind each p65 and p50 homodimer with a 1:1 stoichiometry and with affinities, determined by global analysis, K(d) = 4.8 +/- 0.2 nM for p65 and K(d) = 0.8 +/- 0.2 nM for p50. A global analysis tool for competitive NF-kappa B/Ig kappa binding was developed and utilized to measure the affinity of thioaptamers selected by both p65 and p50. The competition results indicate that the thioaptamers bind and compete for the same NF-kappa B site as the known promoter element Ig kappa B (K(d) = 78.9 +/- 1.9 nM for a p65-selected aptamer and 19.6 +/- 1.3 nM for a p50-selected thioaptamer). Qualitative gel shift binding experiments with p50 also demonstrate that the nature of enhanced affinity and specificity can be attributed to the presence of sulfur. Collectively, these results demonstrate the feasibility of the thioaptamer in vitro combinatorial selection technology as a method for producing specific, high-affinity ligands to proteins.<<
Cheers, Tuck |
