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Updated: May 31, 2026
A Novel In Vitro Wound Healing Assay to Evaluate Cell Migration
Published on: March 17, 2018
Wound healing activity of the human antimicrobial peptide LL37
Reinaldo Ramos1, João Pedro Silva, Ana Cristina Rodrigues
1IBB, Institute of Biotechnology and Bioengineering, Centre of Biological Engineering, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal.
Abstract:
Antimicrobial peptides (AMPs) are part of the innate immune system and are generally defined as cationic, amphipathic peptides, with less than 50 amino acids, including multiple arginine and lysine residues. The human cathelicidin antimicrobial peptide LL37 can be found at different concentrations in many different cells, tissues and body fluids and has a broad spectrum of antimicrobial and immunomodulatory activities. The healing of wound is a complex process that involves different steps: hemostasis, inflammation, remodeling/granulation tissue formation and re-epithelialization. Inflammation and angiogenesis are two fundamental physiological conditions implicated in this process. We have recently developed a new method for the expression and purification of recombinant LL37. In this work, we show that the recombinant peptide P-LL37 with a N-terminus proline preserves its immunophysiological properties in vitro and in vivo. P-LL37 neutralized the activation of macrophages by lipopolysaccharide (LPS). Besides, the peptide induced proliferation, migration and tubule-like structures formation by endothelial cells. Wound healing experiments were performed in dexamethasone-treated mice to study the effect of LL37 on angiogenesis and wound regeneration. The topical application of synthetic and recombinant LL37 increased vascularization and re-epithelialization. Taken together, these results clearly demonstrate that LL37 may have a key role in wound regeneration through vascularization.
Insights
The antimicrobial peptide LL37, when produced recombinantly, promotes wound healing by stimulating blood vessel formation (angiogenesis) and skin regeneration. This peptide shows potential for improving therapeutic strategies for wound repair.
Area of Science:
- Immunology
- Wound Healing Research
- Biochemistry
Background:
- Antimicrobial peptides (AMPs), like human cathelicidin LL37, are crucial for innate immunity.
- LL37 exhibits broad antimicrobial and immunomodulatory functions and is present in various human tissues.
- Wound healing is a complex physiological process involving inflammation and angiogenesis.
Purpose of the Study:
- To evaluate the immunophysiological properties and wound healing potential of a newly developed recombinant LL37 peptide (P-LL37).
- To investigate the effects of P-LL37 on macrophage activation and endothelial cell functions.
- To assess the impact of LL37 on angiogenesis and wound regeneration in vivo.
Main Methods:
- Development of a novel method for expressing and purifying recombinant LL37 (P-LL37).
- In vitro assays to assess P-LL37's effect on lipopolysaccharide-activated macrophages and endothelial cell proliferation, migration, and tubule formation.
- In vivo wound healing experiments in dexamethasone-treated mice using topical application of synthetic and recombinant LL37.
Main Results:
- Recombinant P-LL37 retained its immunophysiological properties, neutralizing LPS-induced macrophage activation.
- P-LL37 stimulated endothelial cell proliferation, migration, and the formation of vascular-like structures.
- Topical LL37 significantly enhanced vascularization and re-epithelialization in mouse wound models.
Conclusions:
- Recombinant LL37 (P-LL37) effectively preserves its biological activities.
- LL37 plays a significant role in promoting wound regeneration by enhancing angiogenesis.
- LL37 demonstrates therapeutic potential for improving wound healing outcomes.
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