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Updated: Oct 2, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
Bacterial type I signal peptidase inhibitors - Optimized hits from nature
Natalia Szałaj1, Andrea Benediktsdottir2, Dominika Rusin1
1Jagiellonian University Medical College, Faculty of Pharmacy, 9 Medyczna St., 30-688, Kraków, Poland.
Abstract:
The ever-increasing number of bacteria resistant to the currently available antibacterial agents is a great medical problem today, and new antibiotics with novel mechanisms of action are urgently needed. Among the validated antibacterial drug targets against which new classes of antibiotics might be directed is bacterial type I signal peptidase (SPase I), an essential part of the Tat and Sec secretory systems. SPase I is responsible for the hydrolysis of the N-terminal signal peptides from proteins secreted across the cytoplasmic membrane and plays a key role in bacterial viability and virulence. This review focuses on the antibacterial activity of natural and synthetic SPase I inhibitors reported to date, namely β-lactams, lipopeptides, and arylomycins, but also an example of SPase I activator was presented.
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