Using Thermal Shift Assays to Identify Inhibitors of the Isocitrate Lyase-1 Protein in Mycobacterium Tuberculosis
Session Number
Project ID: BIO 29
Advisor(s)
Dr. Angela Ahrendt; Illinois Mathematics and Science Academy
Discipline
Biology
Start Date
22-4-2020 10:25 AM
End Date
22-4-2020 10:40 AM
Abstract
Tuberculosis is an airborne respiratory disease that has a high latency period and is caused by the bacteria Mycobacterium tuberculosis. Nearly one third of the world’s population today is infected with this bacteria and approximately 1.3 million people experience tuberculosis related deaths every year. In this study, we chose to examine the isocitrate lyase-1 (ICL-1) protein as a possible target for the treatment of tuberculosis. We took this approach because ICL-1 allows the Mycobacterium tuberculosis bacteria to skip some of the steps in the KREBS cycle, which gives it the ability to survive in low-oxygen environments. The inhibition of ICL-1 could prevent the bacteria from becoming active within the human immune system. Different compounds were tested using a protein thermal shift assay to determine their efficacy in binding to the ICL-1 protein.
Using Thermal Shift Assays to Identify Inhibitors of the Isocitrate Lyase-1 Protein in Mycobacterium Tuberculosis
Tuberculosis is an airborne respiratory disease that has a high latency period and is caused by the bacteria Mycobacterium tuberculosis. Nearly one third of the world’s population today is infected with this bacteria and approximately 1.3 million people experience tuberculosis related deaths every year. In this study, we chose to examine the isocitrate lyase-1 (ICL-1) protein as a possible target for the treatment of tuberculosis. We took this approach because ICL-1 allows the Mycobacterium tuberculosis bacteria to skip some of the steps in the KREBS cycle, which gives it the ability to survive in low-oxygen environments. The inhibition of ICL-1 could prevent the bacteria from becoming active within the human immune system. Different compounds were tested using a protein thermal shift assay to determine their efficacy in binding to the ICL-1 protein.