Research Progress on Stapled Antimicrobial Peptides
Current antimicrobial chemotherapy faces a significant threat from antibiotic resistance,and novel antimicrobial medication architectures or modes of action are desperately needed.Antimicrobial peptides,due to their broad-spectrum antimicrobial activity and unique bactericidal mechanisms,are considered potential therapeutic agents against multidrug-resistant bacteria with good development prospects.However,antimicrobial peptides have disadvantages such as structural instability and susceptibility to proteolytic degradation,which hinder the clinical translation of these peptides.Improving the structural stability of peptides can be achieved by various methods,such as non-natural amino acid modifications and cyclization.In recent years,a particular cyclization method called stapling modification has gained significant attention.This method involves the use of all carbon-hydrogen,triazole or thioether based staples.The addition of stapling structures can enhance antimicrobial activity,improve the stability of antimicrobial peptide structures,especially α-helical structures,and resist proteolytic degradation.However,it may also increase hemolytic side effects.This review introduces the structure,and synthesis of stapled peptides.In an effort to support the creation of novel antimicrobial medications against resistant bacteria,we present instances of stapled antimicrobial peptides in research and go over the key variables affecting their efficacy..
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