Ahn, Jung-Mo

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Jung-Mo Ahn is an Associate Professor of Chemistry, focusing on bio-organic and medicinal chemistry. Through his research he is seeking to understand the chemistry and biology of peptides and proteins, and to develop new approaches for manipulating these properties with purposefully designed small organic molecules. His projects include:

  • Development of peptidomimetics for the treatment of Diabetes Mellitus
  • Development of therapeutic agents for biodefense against bacterial infection
  • Rational design of small molecules for mimicking protein secondary structures to modulate protein-protein interactions involved in cancer
  • Development of metabolically stable peptides as molecular imaging agents for non-invasive assessment of pancreatic beta-cells

Learn more about Dr. Ahn at his Faculty and Research as well as his Research Explorer pages.


Recent Submissions

Now showing 1 - 2 of 2
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    Estrogen Receptor Coregulator Binding Modulators (ERXs) Effectively Target Estrogen Receptor Positive Human Breast Cancers
    (2017-08-08) Raj, Ganesh V.; Sareddy, Gangadhara Reddy; Ma, Shihong; Lee, Tae-Kyung; Viswanadhapalli, Suryavathi; Li, Rui; Liu, Xihui; Murakami, Shino; Chen, Chien-Cheng; Lee, Wan-Ru; Mann, Monica; Krishnan, Samaya Rajeshwari; Manandhar, Bikash; Gonugunta, Vijay K.; Strand, Douglas; Tekmal, Rajeshwar Rao; Ahn, Jung-Mo; Vadlamudi, Ratna K.; Lee, Tae-Kyung; Manandhar, Bikash; Ahn, Jung-Mo
    The majority of human breast cancer is estrogen receptor alpha (ER) positive. While anti-estrogens/aromatase inhibitors are initially effective, resistance to these drugs commonly develops. Therapy-resistant tumors often retain ER signaling, via interaction with critical oncogenic coregulator proteins. To address these mechanisms of resistance, we have developed a novel ER coregulator binding modulator, ERX-11. ERX-11 interacts directly with ER and blocks the interaction between a subset of coregulators with both native and mutant forms of ER. ERX-11 effectively blocks ER-mediated oncogenic signaling and has potent anti-proliferative activity against therapy-sensitive and therapy-resistant human breast cancer cells. ERX-11 is orally bioavailable, with no overt signs of toxicity and potent activity in both murine xenograft and patient-derived breast tumor explant models. This first-in-class agent, with its novel mechanism of action of disrupting critical protein-protein interactions, overcomes the limitations of current therapies and may be clinically translatable for patients with therapy-sensitive and therapy-resistant breast cancers.
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    FK228 Analogues Induce Fetal Hemoglobin in Human Erythroid Progenitors
    (2012-03-07) Makala, L.; Di Maro, Salvatore; Lou, Tzu-Fang; Sivanand, S.; Ahn, Jung-Mo; Pace, B. S.
    Fetal hemoglobin (HbF) improves the clinical severity of sickle cell disease (SCD), therefore, research to identify HbF-inducing agents for treatment purposes is desirable. The focus of our study is to investigate the ability of FK228 analogues to induce HbF using a novel KU812 dual-luciferase reporter system. Molecular modeling studies showed that the structure of twenty FK228 analogues with isosteric substitutions did not disturb the global structure of the molecule. Using the dual-luciferase system, a subgroup of FK228 analogues was shown to be inducers of HbF at nanomolar concentrations. To determine the physiological relevance of these compounds, studies in primary erythroid progenitors confirmed that JMA26 and JMA33 activated HbF synthesis at levels comparable to FK228 with low cellular toxicity. These data support our lead compounds as potential therapeutic agents for further development in the treatment of SCD. © 2012 Levi Makala et al.

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