Abby Ho

University of Kentucky, Lexington, Kentucky, United States

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Publications (4)9.13 Total impact

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    ABSTRACT: The major estrogen metabolite 2-methoxyestradiol (2ME) has been shown to target tumor cells without severe side effects and is currently being evaluated in clinical trials for several types of cancer. Despite its promise for use in clinical setting, the mechanism(s) by which 2ME exerts its anti-tumor activity is not clearly defined at this time. Employing organic chemistry tools, we synthesized 2ME analogs with which 2ME affinity column was prepared, enabling us to detect a protein that selectively interacts with 2ME. This 2ME analog will be useful as a probe to identify the biological target(s) of 2ME and study their functions in tumor cells.
    No preview · Article · Aug 2006 · Bioorganic & Medicinal Chemistry Letters
  • Abby Ho · Kedra Cyrus · Kyung‐Bo Kim
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    ABSTRACT: Eponemycin, an antitumor and antiangiogenic epoxy ketone natural product, is previously shown to target proteasome for its activity. Although there have been many synthetic approaches developed, practical and efficient synthetic strategy for eponemycin has yet to be accomplished. Here, we report an efficient new route for the preparation of dihydroeponemycin, an active eponemycin derivative. This will aid the design of proteasome inhibitors with novel activity. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005)
    No preview · Article · Nov 2005 · European Journal of Organic Chemistry
  • D Zhang · S-H Baek · A Ho · H Lee · Y S Jeong · K Kim
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    ABSTRACT: A novel strategy that targets protein for degradation has recently been developed by exploiting a protein-targeting chimeric molecule ('Protac'). Typically, the chimeric Protac is composed of a small-molecule ligand ('bait') on one end and a synthetic octapeptide on the other. This octapeptide is recognized by E3 ubiquitin ligase pVHL (von Hippel Lindau tumor suppressor protein), thereby recruiting a small molecule-bound protein ('prey') to pVHL for ubiquitination and degradation. Since selective degradation of a cellular protein generates a "loss of function" mutation, this protein knock-out strategy may be useful to study the function of a given protein or to evaluate whether a cellular protein is a potential target for drug intervention, in a manner reminiscent of gene knock-out or siRNA approaches. Herein, we show that a synthetic pentapeptide is sufficient to interact with pVHL E3 ligase, and that the pentapeptide-based Protac efficiently induces ubiquitination and degradation of target protein. Our results also demonstrate that the pentapeptide-based Protac can enter cells efficiently to exerts its biological activity effectively. These results suggest that the synthetic pentapeptide can be used either directly in the preparation of cell-permeable Protacs or as a template to develop peptidomimetic or non-peptide Protacs.
    No preview · Article · Dec 2004 · Combinatorial Chemistry & High Throughput Screening
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    ABSTRACT: Ubiquitin-dependent proteolysis of cellular proteins is one of the major pathways to regulate protein function posttranslationally. Here we demonstrate a potentially general method of degrading any targeted proteins by the ubiquitin-dependent proteolysis in living cells, using small-molecule proteolysis inducer (SMPI).
    No preview · Article · Mar 2004 · Bioorganic & Medicinal Chemistry Letters