Skip NavigationSkip to Content
Return Return to Search Results

Synthesis, anti-cancer screening and tyrosyl-DNA phosphodiesterase 1 (Tdp1) inhibition activity of novel piperidinyl sulfamides

  1. Author:
    Jun, Jung Ho
    Kumar, Vineet
    Dexheimer, Thomas S
    Wedlich, Iwona
    Nicklaus, Marc
    Pommier, Yves
    Malhotra, Sanjay V

  2. Author Address

    Department of Chemistry, University of Kansas, KS 66045, USA., Department of Radiation Oncology, Stanford University, 3165 Porter Drive, Palo Alto, CA 94304, USA., Laboratory of Molecular Pharmacology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, 20892, USA., Chemical Biology Laboratory, Frederick National Laboratory for Cancer Research, 376 Boyles Street, Frederick, MD 21702, USA., Department of Radiation Oncology, Stanford University, 3165 Porter Drive, Palo Alto, CA 94304, USA. Electronic address: smalhotra@stanford.edu.,
    1. Year: 2018
    2. Date: Jan 01
    3. Epub Date: 2017 10 13
  2. Journal: European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences
    1. 111
    2. Pages: 337-348
  4. Type of Article: Article
  1. Abstract:

    Novel piperidinyl-based sulfamide derivatives were designed and synthesized through various synthetic routes. Anticancer activities of these sulfamides were evaluated by phenotypic screening on National Cancer Institute's 60 human tumor cell lines (NCI-60). Preliminary screening at 10µM concentration showed that piperidinyl sulfamide aminoester 26 (NSC 749204) was sensitive to most of the cell lines in the panel. Further dose-response studies showed that 26 was highly selective for inhibition of colon cancer cell lines with minimum GI50=1.88µM for COLO-205 and maximum GI50=11.1µM for SW-620 cells. These newly synthesized sulfamides were also screening for their Tdp1 inhibition activity. Compound 18 (NSC 750706) showed significant inhibition of Tdp1 with IC50=23.7µM. Molecular-docking studies showed that 18 bind to Tdp1 in its binding pocket similar to a known Tdp1 inhibitor. Copyright © 2017. Published by Elsevier B.V.

    See More

  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1016/j.ejps.2017.10.017
  3. PMID: 29037996
  4. View record in Web of Science®
  5. WOS: 000415120300037
  6. PII : S0928-0987(17)30561-4

Library Notes

  1. Fiscal Year: FY2017-2018
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel