Study summary · research use only
Design of Antimicrobial Peptides: Progress Made with Human Cathelicidin LL-37
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This review discusses design of antimicrobial peptides based on human cathelicidin LL-37, part of human innate immunity, describing alternative processing of the human cathelicidin precursor, protease digestion, and identification of LL-37's core antimicrobial region through synthetic peptide libraries, structure-based design, and determination of its 3D structure. The authors describe LL-37 as engineered into 17BIPHE2, and note that both 17BIPHE2 and SAAP-148 were reported in cited studies to eliminate ESKAPE pathogens and to show topical antibiofilm activity in vivo. The review discusses potential applications of LL-37-derived peptides as antibacterial, antibiofilm, antiviral, antifungal, immune-modulating, and anticancer agents, along with related strategies such as peptide formulation, antimicrobial implants, and peptide-inducing factors including vitamin D and sunlight.
Abstract
The incorporation of the innate immune system into humans is essential for survival and health due to the rapid replication of invading microbes and the delayed action of the adaptive immune system. Antimicrobial peptides are important components of human innate immunity. Over 100 such peptides have been identified in various human tissues. Human cathelicidin LL-37 is best studied, and there has been a growing interest in designing new peptides based on LL-37. This chapter describes the alternative processing of the human cathelicidin precursor, protease digestion, and lab cutting of LL-37. Both a synthetic peptide library and structure-based design are utilized to identify the active regions. Although challenging, the determination of the 3D structure of LL-37 enabled the identification of the core antimicrobial region. The minimal region of LL-37 can be function-dependent. We discuss the design and potential applications of LL-37 into antibacterial, antibiofilm, antiviral, antifungal, immune modulating, and anticancer peptides. LL-37 has been engineered into 17BIPHE2, a stable, selective, and potent antimicrobial, antibiofilm, and anticancer peptide. Both 17BIPHE2 and SAAP-148 can eliminate the ESKAPE pathogens and show topical in vivo antibiofilm efficacy. Also discussed are other application strategies, including peptide formulation, antimicrobial implants, and peptide-inducing factors such as vitamin D and sunlight. Finally, we summarize what we learned from peptide design based on human LL-37.
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