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Updated: Sep 10, 2025

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
Current advances and emerging prospects of specifically targeted antimicrobial peptides: A comprehensive review
Jiajia Qiu1, Deyang Wu2, Chong Xu3
1Food Nutrition and Health Research Center, School of Advanced Manufacturing, Fuzhou University, Jinjiang, Fujian 362200, China; Institute of Food Science and Technology, College of Biological Science and Engineering, Fuzhou University, Fuzhou, Fujian 350108, China.
Abstract:
To prevent the indiscriminate impact of traditional antimicrobials on both harmful and beneficial microbes in the host, specifically targeted antimicrobial peptides (STAMPs) have been designed and developed. This review provides a comprehensive summary of recent advancements in STAMPs, with an emphasis on their structure, antimicrobial activity, design strategies, applications, challenges, and future prospects. STAMPs are composed of targeting, linker, and killing domains, which facilitate the precise elimination of specific pathogens while minimizing impacts on non-targeted microorganisms. The targeting domain of STAMP is of critical importance, as it confers specificity in the recognition and binding to pathogens. Current design strategies for targeting domain employ bacterial pheromones, receptor-binding proteins (RBPs) from bacteriophages, antibodies, and specific binding peptides. STAMPs demonstrate significant potential across various fields, including clinical medicine, agriculture, biomaterials, and food preservation. Although numerous challenges remain, advancements in computer-aided design (CAD) and synthetic biology are expected to significantly facilitate the rational design and production of STAMPs.
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