CLC number: O657.63
On-line Access: 2024-08-27
Received: 2023-10-17
Revision Accepted: 2024-05-08
Crosschecked: 0000-00-00
Cited: 0
Clicked: 5388
ZHANG Hong, PAN Yuan-jiang. Affinity ultrafiltration of DNA topoisomerases-targeted compounds determined with HPLC/ESI-MS for drug candidate screening[J]. Journal of Zhejiang University Science A, 2004, 5(8): 900-905.
@article{title="Affinity ultrafiltration of DNA topoisomerases-targeted compounds determined with HPLC/ESI-MS for drug candidate screening",
author="ZHANG Hong, PAN Yuan-jiang",
journal="Journal of Zhejiang University Science A",
volume="5",
number="8",
pages="900-905",
year="2004",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.2004.0900"
}
%0 Journal Article
%T Affinity ultrafiltration of DNA topoisomerases-targeted compounds determined with HPLC/ESI-MS for drug candidate screening
%A ZHANG Hong
%A PAN Yuan-jiang
%J Journal of Zhejiang University SCIENCE A
%V 5
%N 8
%P 900-905
%@ 1869-1951
%D 2004
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2004.0900
TY - JOUR
T1 - Affinity ultrafiltration of DNA topoisomerases-targeted compounds determined with HPLC/ESI-MS for drug candidate screening
A1 - ZHANG Hong
A1 - PAN Yuan-jiang
J0 - Journal of Zhejiang University Science A
VL - 5
IS - 8
SP - 900
EP - 905
%@ 1869-1951
Y1 - 2004
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2004.0900
Abstract: A method of screening assay is demonstrated. The approach is based on the affinity of antitumor candidates for topoi-somerases. In this method, antitumor candidates are fished out using topoisomerases as targets. Traditional analysis of complex compounds typically encounters signal suppression due to the relatively low concentrations, but enzyme-affinity screening for the active compounds can effectively concentrate the desired analysts into a small volume of high concentration. Active compounds are separated from non-affinity compounds by ultrafiltration. The molecules-enzymes complexes that are retained on the filter are subsequently separated by acidification to obtain the topoisomerases-affinity compounds for analysis on High Performance Liquid Chromatography coupled with electrospray ionization mass spectrometric detection (ESI-MS). This enzyme-affinity based screening assay provides a highly specific and efficient method that can directly screen, identify, and acquire drug candidates thus improving the accuracy and speed of high-throughput screening activities.
[1] Bjergbaek, L., Kingma, P., Nielsen, I.S., Wang, Y., Werstergaard, O., Osheroff, N., Andersen, A.H., 2000. Communication between the ATPase and cleavage/religation domains of human topoisomerase II alpha. J Biol Chem, 275:13041-13048.
[2] Brimmel, C.L., Vickennan, J.C., Cart, S.A., 1996. Evaluation of mass spectrometric methods applicable to the direct analysis of non-peptide beed-bound combinatorial libraries. Anal Chem, 68:237-242.
[3] Burbaum, J., 1998. Miniaturization technologic in HTS: how fast, how small, how soon. Drug Discovery Today, 3:313-322.
[4] Chang, J.Y., Dethlefsen, L.A., Barley, L.R., Zhou, B.S., Cheng, Y.S., 1992. Characterization of camptothecin resistant Chinese hamster lung cells. Biochem Pharmacology, 43:2443-2452.
[5] De Isabella, P., Capranico, G., Binaschi, M., Tinelli, S., Zunino, F., 1990. Evidence of topoisomerase II-dependent mechanisms of multidrug resistance in p388 leukemia cells. Mol. Pharmacol, 37:11.
[6] Froelich, A.S.J., Osheroff, N., 1995. Topoisomerase poisons: harnessing the dark side of enzyme mechanism. J Biol Chem, 270:21429-21432.
[7] Gund, P., Nolan, H.S., 1999. Applying informatics systems to high-throughput screening and analysis. Phamainformatics, 1:25-29.
[8] Hengel, A.J.V., Harkes, M.P., Wichers, H.J., 1992. Characterization of callus formation and camptothecin production by cell lines of Camptotheca acuminate. Plant Cell, Tissue and Organ Culture, 28:11-18.
[9] Husain, I., Mohler, J.L., Siegler, H.F., Besterman, J.M., 1994. Elevation of topoisomerase I messenger RNA, protein, and catalytic activity in human tumors: demonstration of tumor-type specificity and implications for cancer chemotherapy. Cancer Research, 54:539-546.
[10] Kaufmann, S.H., Charron, M., Burke, P.J., Karp, J.E., 1995. Changes in topoisomerase I levels and localization during myeloid maturation in vitro and in vivo. Cancer Research, 55:1255-1260.
[11] Liu, X., 1992. Study on anti-tumors drugs which affect on DNA topoisomerases. Oversea Medical Science, 19:201-205 (in Chinese).
[12] Li, Y.Y., Li, Z.Y., Wang, H., You, Q.D., 1996. DNA topoisomerases and anticancer drugs. Pharmic Advance, 20:138-142 (in Chinese).
[13] Major, J., 1998. Challenges and opportunities in high throughput screening: implication for new technologies. J Biomol Screening, 3:13-17.
[14] Meng, L.H., Zhang, J.S., Ding, J., 2001. Salvicine, a novel DNA topoisomerase II inhibitor, exerting its effects by trapping enzyme-DNA cleavage complexes. Biochem. Pharmaco., 62:733-741.
[15] Sundberg, S.A., 2000. High-throughput and ultra-high throughput screening: solution- and cell-based approaches. Current Opinion in Biotechnology, 11:47-53.
[16] Wang, J.C., 1996. DNA Topoisomerases. Annu Rev Biochem, 65:635-692.
[17] Wang, Y., Thyssen, A., Westergaard, O., Andersen, A.H., 2000. Position-specific effect of ribonucleotides on the cleavage activity of human topoisomerase II. Nucleic Acids Res, 28:4815-4821.
[18] Wiehodt, R., Zweigenbaum, J., Henion, J., 1997. Immunoaffinity ultrafiltration with ion spray HPLC/Ms for screening small-molecule libraries. Anal Chem, 69:1683-1691.
Open peer comments: Debate/Discuss/Question/Opinion
<1>