ATP Synthase: The Future of Antibiotics

By: Keiko P

Published on: January 13th, 2024

ATP Synthase is an enzyme essential for many animal bodily functions, it assists in producing ATP, an important molecule responsible for storing and releasing energy. ATP is necessary for a variety of functions, such as transporting substances across membranes and moving muscles.

ATP Synthase transforms Adenosine Diphosphate (ADP) and a phosphate group into Adenosine Triphosphate (ATP), where it can then do its duty and supply the required energy to the different components of the body. All enzymes, including ATP Synthase, act as catalysts, they are not used up during the transformation process and can be reused to perform the transformation. This means that the enzyme can perform its job indefinitely unless certain restrictions are applied (such as inhibitors).

The ideal conditions for ATP synthase relate to its ability to accept ADP and Pi. The enzyme was found to perform best when interacting with an auxiliary buffering enzyme, like adenylate kinase, and at a pH level of around 7. This is because they are a tool for directing protons to molecular targets, such as ATP Synthase. This allows for ATP Synthase to intake as much material as possible and catalyze it into ATP efficiently.

ATP Synthase is typically found in the membrane of the mitochondria, the powerhouse of the cell. The mitochondria are responsible for providing energy to the cell using ATP. This correlates with the presence of ATP Synthase in the mitochondria, as it creates the ATP that the mitochondria then distribute based on the needs of the cell.

The enzyme can also be located in the plasma membrane of bacteria. Developments have been made to suggest that the inhibitors of ATP Synthase could be used as a form of antibiotics that could target certain resistant bacteria, as they would slow the production of energy to the bacteria, therefore hindering its ability to thrive. The pharmaceutical and therapeutic industries have worked tirelessly over the years to develop a “natural” biologically effective antibiotic that can prolong the effectiveness of antibiotics for resistant bacteria, and the ATP Synthase inhibitor is a reasonable prospect. By introducing ATP Synthase inhibitors into the bacteria environment, researchers found that they were able to inhibit the catalyzation of ADP and Pi into ATP, which therefore means that less required energy was provided to the bacteria cell, eventually killing it.

Researchers have discovered that when a bacteria has grown resistant to the typical antibiotic treatments, introducing ATP Synthase inhibitors may help to kill off the bacteria once it has become resistant. This is very beneficial, as finding effective antibiotics that work despite any resistance is difficult.

Overall, ATP Synthase inhibitors open a realm of possibilities for the pharmaceutical industry and could be a helpful antibiotic that works towards saving lives.

Works Cited

Pertuzello, M. (2024, August 16). Adenosine triphosphate (ATP) | Definition, Structure, Function, & Facts. Britannica. Retrieved September 27, 2024, from https://www.britannica.com/science/adenosine-triphosphate

Igamberdiev, A. & Kleczkowski, L. (2015, June 10). Optimization of ATP synthase function in mitochondria and chloroplasts via the adenylate kinase equilibrium. National Library of Medicine. Retrieved September 30, 2024 from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4309032/

Yoshida, M., Muneyuki, E. & Hisabori, T. (2001, September 1). ATP synthase — a marvellous rotary engine of the cell. Nature. Retrieved September 27, 2024 from https://www.nature.com/articles/35089509

Mackieh, R., Al-Bakkar, N., Kfoury, M., Roufayel, R., Sabatier, J. & Fajloun Z. (2023, March 24). Inhibitors of ATP Synthase as New Antibacterial Candidates. MDPI. Retrieved September 27, 2024 from https://www.mdpi.com/2079-6382/12/4/650