ReviewInternational journal of molecular sciences2025
Antimicrobial Peptides of the Cathelicidin Family: Focus on LL-37 and Its Modifications.
Review in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed.
- Impact of cathelicidin cleavage by SpeB onbioRxiv : the preprint server for biology · 2026Article
- Engineering Smart Scaffolds for Osteomyelitis: Integrating Nanotechnology, Drug Delivery, and Tissue Regeneration-A Narrative Review.Journal of functional biomaterials · 2026Review
- Exploratory Evaluation of Susceptibility Patterns of Clinical Isolates ofAntibiotics (Basel, Switzerland) · 2026Article
- Unlocking the potential of cyclic peptides in bioactive wound dressings for enhanced tissue repair.Molecular biology reports · 2026Review
- SA-MTP: a structure-aware framework for multifunctional therapeutic peptide annotation.Briefings in bioinformatics · 2026Article
- Review
- Article
- Overcoming LPS-mediated resistance in gram-negative pathogens: a review of LL-37 analogs and computational design strategies.Archives of microbiology · 2026Review
- Optimized LL-37-Derived Peptides Exhibit Antitubercular Activity, Induce Membrane Disruption, and P-Type ATPase Transcriptional Responses inBiomolecules · 2026Article
- A One Health Perspective onMicroorganisms · 2026Review
- Natural and Synthetic Peptides as Alternatives to Antibiotics in Intestinal Infections-A Review.Antibiotics (Basel, Switzerland) · 2026Review
- Immune cell dynamics and cytokine regulation in cornea and transplantation.Frontiers in immunology · 2026Review
- Antibacterial Immunotherapy: Mechanistic Insights, Emerging Therapeutic Strategies, and Clinical Translation.Infection and drug resistance · 2026Review
- Vitamin D-AMP axis in host defense against fungal infections.Frontiers in nutrition · 2026Review
- Therapeutic strategies against biofilm-associated multidrug-resistantFrontiers in microbiology · 2026Review
- Differential antimicrobial activity of two LL37 derivatives against periodontal bacteria, including enhanced efficacy againstFrontiers in microbiology · 2026Article
- Vitamin D3-Deficient Diet Promotes Pulmonary Fibrosis Development in Murine Model of Hypersensitivity Pneumonitis.International journal of molecular sciences · 2025Article
- Virtual Screening of Cathelicidin-Derived Anticancer Peptides and Validation of Their Production in the ProbioticInternational journal of molecular sciences · 2025Article
- Elevated Serum LL37 and Myeloperoxidase-DNA Complexes Predict the Progression of Diabetic Kidney Disease.Kidney diseases (Basel, Switzerland)Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.