Skip NavigationSkip to Content
Return Return to Search Results

Examination of phosphoryl-mimicking functionalities within a macrocyclic Grb2 SH2 domain-binding platform

  1. Author:
    Kang, S. U.
    Shi, Z. D.
    Worthy, K. M.
    Bindu, L. K.
    Dharmawardana, P. G.
    Choyke, S. J.
    Bottaro, D. P.
    Fisher, R. J.
    Burke, T. R.

  2. Author Address

    NCI, Med Chem Lab, Ctr Canc Res, NIH, Frederick, MD 21702 USA. SAIC Frederick, Prot Chem Lab, Frederick, MD 21702 USA. NCI, Ctr Canc Res, Urol Oncol Branch, NIH, Bethesda, MD 20892 USA Burke, TR, NCI, Med Chem Lab, Ctr Canc Res, NIH, Frederick, MD 21702 USA
    1. Year: 2005
    2. Date: JUN 16
  2. Journal: Journal of Medicinal Chemistry
    1. 48
    2. 12
    3. Pages: 3945-3948
  4. Type of Article: Article
  1. Abstract:

    Reported herein are the design, synthesis, and Grb2 SH2 domain-binding affinities of several phosphoryl-mimicking groups displayed within the context of a conformationally constrained macrocyclic platform. With use of surface plasmon resonance techniques, single-digit nanomolar affinities were exhibited by phosphonic acid and malonyl-containing diacidic phosphoryl mimetics (for 4h and 4g, K-D = 1.47 and 3.62 nM, respectively). Analogues containing monoacidic phosphoryl mimetics provided affinities of K-D = 16-67 nM. Neutral phosphoryl-mimicking groups did not show appreciable binding

    See More

  1. Keywords:

External Sources

  1. View record in Web of Science®
  2. WOS: 000229805000003

Library Notes

  1. No notes added.
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