Presenter Information

Oliwia OzogFollow

Major

Chemistry

Anticipated Graduation Year

2020

Access Type

Open Access

Abstract

In the 21st century, a global antibacterial resistance crisis has risen and is threatening the lives of millions. In addition, it has been determined that antibiotic resistance has added tremendous financial and clinical burdens on the U.S. health care system, patients and their families. The rise of this crisis has in part been attributed to the lack of new drug developments in the field of antibiotics as well as the overuse and misuse of existing medications. A novel bacterial pathway must be discovered and exploited in the fight to combat the antibiotic resistance crisis. DapE is an essential bacterial enzyme in the biosynthetic pathway responsible for the production of meso-diaminopimelic acid (m-DAP) and the amino acid lysine, which are critical to bacterial survival. DapE is an ideal drug target because the human body does not employ the DapE enzyme to manufacture lysine; humans must consume lysine in their diets. Thus, the elimination of mechanism-based toxicity, combined with the discovery of multiple potential inhibitors in our lab for this enzyme, makes DapE a great target to focus on toward the discovery of new antibiotics. This research has proven to be fruitful, but little is known about DapE and its properties. Synthesis of disulfonates will advance our understanding of the DapE enzyme in exploring the impact of a conformational change triggered by substrate binding means for the catalytic mechanism of the DapE enzyme.

Faculty Mentors & Instructors

Daniel P. Becker, Ph.D. Department of Chemistry and Biochemistry

Creative Commons License

Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.

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Synthesis of Disulfonates as DapE Inhibitors Toward the Creation of Novel Antibiotics

In the 21st century, a global antibacterial resistance crisis has risen and is threatening the lives of millions. In addition, it has been determined that antibiotic resistance has added tremendous financial and clinical burdens on the U.S. health care system, patients and their families. The rise of this crisis has in part been attributed to the lack of new drug developments in the field of antibiotics as well as the overuse and misuse of existing medications. A novel bacterial pathway must be discovered and exploited in the fight to combat the antibiotic resistance crisis. DapE is an essential bacterial enzyme in the biosynthetic pathway responsible for the production of meso-diaminopimelic acid (m-DAP) and the amino acid lysine, which are critical to bacterial survival. DapE is an ideal drug target because the human body does not employ the DapE enzyme to manufacture lysine; humans must consume lysine in their diets. Thus, the elimination of mechanism-based toxicity, combined with the discovery of multiple potential inhibitors in our lab for this enzyme, makes DapE a great target to focus on toward the discovery of new antibiotics. This research has proven to be fruitful, but little is known about DapE and its properties. Synthesis of disulfonates will advance our understanding of the DapE enzyme in exploring the impact of a conformational change triggered by substrate binding means for the catalytic mechanism of the DapE enzyme.