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Structure-Based Optimization of Protein Tyrosine Phosphatase 1B Inhibitors: From the Active Site to the Second Phosphotyrosine Binding Site
Open accessAbstract
Protein tyrosine phosphatase 1B (PTP1B) is a negative regulator of the insulin and leptin receptor pathways and thus an attractive therapeutic target for diabetes and obesity. Starting with a high micromolar lead compound, structure-based optimization of novel PTP1B inhibitors by extension of the molecule from the enzyme active site into the second phosphotyrosine binding site is described. Medicinal chemistry, guided by X-ray complex structure and molecular modeling, has yielded low nanomolar PTP1B inhibitors in an efficient manner. Compounds from this chemical series were found to be actively transported into hepatocytes. This active uptake into target tissues could be one of the possible avenues to overcome the poor membrane permeability of PTP1B inhibitors.
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Cites
Klaman, L. D., Boss, O., Peroni, O. D., Kim, J. K., Martino, J. L., Zabolotny, J. M., Moghal, N., Lubkin, M., Kim, Y.-B., Sharpe, A. H., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5479-5489.2000 · Cited by 1,235
Cited by
Wang, L., Wu, Y., Deng, Y., Kim, B., Pierce, L., Krilov, G., Lupyan, D., Robinson, S., Dahlgren, M. K., Greenwood, J., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/ja512751q · Cited by 1,313
Assessment of Binding Affinity via Alchemical Free-Energy Calculations
Kuhn, M., Firth-Clark, S., Tosco, P., Mey, A. S. J. S., Mackey, M., & Michel, J. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00165 · Cited by 222
Metadata
- Authors
- Wilson, D. P., Wan, Z.-K., Xu, W.-X., Kirincich, S. J., Follows, B. C., Joseph-McCarthy, D., Foreman, K., Moretto, A., Wu, J., Zhu, M., Binnun, E., Zhang, Y.-L., Tam, M., Erbe, D. V., Tobin, J., Xu, X., Leung, L., Shilling, A., Tam, S. Y., Mansour, T. S., & Lee, J.
- Venue
- Journal of Medicinal Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-08-17
- Volume
- 50
- Issue
- 19
- Pages
- 4681-4698
- ISSN
- 0022-2623 (ISSN-L)
- 1520-4804
- OpenAlex
- W2091286894
- Cited by
- 160
- References
- 1
- FWCI
- 2.16
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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