Study summary · research use only
Antimicrobial Peptides of the Cathelicidin Family: Focus on LL-37 and Its Modifications
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This review discusses the cathelicidin family of antimicrobial peptides, focusing on the human peptide LL-37 and design strategies used to modify it. The authors describe LL-37 as having antimicrobial, antiviral, antifungal, antiparasitic, and antitumor properties reported in the literature, while noting its clinical application is limited by low proteolytic stability, cytotoxicity, and high production costs. The review summarizes chemical and structural modification strategies, including truncated and retro-analogs described as preserving or improving biological activity while reducing toxicity and increasing proteolytic resistance, and nanoscale delivery systems intended to enable targeted delivery, extend peptide half-life, and reduce cytotoxic effects. The authors state further research, including long-term evaluation, is needed.
Abstract
Cathelicidins are a family of antimicrobial peptides (AMPs) with broad-spectrum activity and immunomodulatory functions. Among them, the only human cathelicidin LL-37 has garnered significant interest due to its potent antimicrobial, antiviral, antifungal, antiparasitic, and antitumor properties. However, the clinical application of LL-37 is hindered by several limitations, including low proteolytic stability, cytotoxicity, and high production costs. To overcome these challenges, a wide range of design strategies have been employed to modify LL-37 and improve its therapeutic potential. LL-37-based analogs represent promising candidates for the development of next-generation antimicrobial and immunomodulatory therapies. Despite significant progress, further research is required to optimize peptide design, ensure cost-effective production, and validate long-term safety and efficacy. Advances in computational modeling, high-throughput screening, and nanotechnology will play an important role in the translation of modified cathelicidins into clinical practice. This review summarizes key strategies of chemical and structural modifications of LL-37 aimed at enhancing its functional properties. Particular attention is given to truncated and retro-analogs, which preserve or improve biological activity while exhibiting reduced toxicity and increased proteolytic resistance. Furthermore, we highlight the use of nanoscale delivery systems, which facilitate targeted delivery, prolong peptide half-life, and mitigate cytotoxic effects.
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