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Examination of acylated 4-aminopiperidine-4-carboxylic acid residues in the phosphotyrosyl+1 position of Grb2 SH2 domain-binding tripeptides

  1. Author:
    Kang, S. U.
    Choi, W. J.
    Oishi, S.
    Lee, K.
    Karki, R. G.
    Worthy, K. M.
    Bindu, L. K.
    Nicklaus, M. C.
    Fisher, R. J.
    Burke, T. R.

  2. Author Address

    NCI, Canc Res Ctr, Med Chem Lab, NIH, Frederick, MD 21702 USA. Sci Applicat Int Corp, Prot Chem Lab, Frederick, MD 21702 USA.;Burke, TR, NCI, Canc Res Ctr, Med Chem Lab, NIH, POB B,Bldg 376 Boyles St, Frederick, MD 21702 USA.;tburke@helix.nih.gov
    1. Year: 2007
    2. Date: Apr
  2. Journal: Journal of Medicinal Chemistry
    1. 50
    2. 8
    3. Pages: 1978-1982
  4. Type of Article: Article
  5. ISSN: 0022-2623
  1. Abstract:

    A 4-aminopiperidine-4-carboxylic acid residue was placed in the pTyr+1 position of a Grb2 SH2 domain-binding peptide to form a general platform, which was then acylated with a variety of groups to yield a library of compounds designed to explore potential binding interactions, with protein features lying below the beta D strand. The highest affinities were obtained using phenylethyl carbamate and phenylbutyrylamide functionalities.

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External Sources

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  2. DOI: 10.1021/jm0614073
  3. View record in Web of Science®
  4. WOS: 000245634500026

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