Major

Chemistry

Research Abstract

With an increase of MRSA (Methicillin-resistant Staphylococcus Aureus) caused hospitalizations, there is a need to explore novel antibiotics against this bacterial induced illness. However, because of the nature of MRSA, the development of new antibiotics could inevitably lead to new resistance in S. aureus, creating a more powerful “superbug”. Therefore, it is paramount to evaluate and explore novel pathways of drug treatment against this bacteria. Sortase A, a cysteine protease of S. aureus, enables it to maintain virulence from its functionality of covalently attaching surface proteins, responsible for the adhesion ability for infection. Inhibitory studies of this enzyme have gained prominent interest as a new pathway of drug development. Through the use of docking software, we have evaluated possible structures that can covalently inhibit Sortase A, which we plan to synthesize and study in future further research.

Faculty Mentor/Advisor

Herman Nikolayevskiy

Available for download on Sunday, January 01, 2040

Included in

Chemistry Commons

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May 7th, 12:00 AM May 10th, 12:00 AM

Covalent Inhibition Against Sortase A Activity in Staphylococcus aureus Bacteria

With an increase of MRSA (Methicillin-resistant Staphylococcus Aureus) caused hospitalizations, there is a need to explore novel antibiotics against this bacterial induced illness. However, because of the nature of MRSA, the development of new antibiotics could inevitably lead to new resistance in S. aureus, creating a more powerful “superbug”. Therefore, it is paramount to evaluate and explore novel pathways of drug treatment against this bacteria. Sortase A, a cysteine protease of S. aureus, enables it to maintain virulence from its functionality of covalently attaching surface proteins, responsible for the adhesion ability for infection. Inhibitory studies of this enzyme have gained prominent interest as a new pathway of drug development. Through the use of docking software, we have evaluated possible structures that can covalently inhibit Sortase A, which we plan to synthesize and study in future further research.