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The Host Defence Peptide LL-37 is Susceptible to Proteolytic Degradation by Wound Fluid Isolated from Foot Ulcers of Diabetic Patients
- Source :
- International Journal of Peptide Research and Therapeutics. 20:457-464
- Publication Year :
- 2014
- Publisher :
- Springer Science and Business Media LLC, 2014.
-
Abstract
- The pleiotropic effects of host defence peptides (HDPs), including the ability to kill microorganisms, enhance re-epithelialisation and increase angiogenesis, indicates a role for these important peptides as potential therapeutic agents in the treatment of chronic, non-healing wounds. However, the maintenance of peptide integrity, through resistance to degradation by the array of proteinases present at the wound site, is a prerequisite for clinical success. In this study we explored the degradation of exogenous LL-37, one such HDP, by wound fluid from diabetic foot ulcers to determine its susceptibility to proteolytic degradation. Our results suggest that LL-37 is unstable in the diabetic foot ulcer microenvironment. Following overnight treatment with wound fluid, LL-37 was completely degraded. Analysis of cleavage sites suggested potential involvement of both host- and bacterial-derived proteinases. The degradation products were shown to retain some antibacterial activity against Pseudomonas aeruginosa but were inactive against Staphylococcus aureus. In conclusion, our data suggest that stabilising selected peptide bonds within the sequence of LL-37 would represent an avenue for future research prior to clinical studies to address its potential as an exogenously-applied therapeutic in diabetic wounds.
- Subjects :
- chemistry.chemical_classification
Angiogenesis
Pseudomonas aeruginosa
medicine.medical_treatment
Bioengineering
Peptide
Biology
medicine.disease
medicine.disease_cause
Biochemistry
Diabetic foot
Analytical Chemistry
Cathelicidin
Microbiology
Diabetic foot ulcer
chemistry
Staphylococcus aureus
Diabetes mellitus
Drug Discovery
medicine
Molecular Medicine
Subjects
Details
- ISSN :
- 15733904 and 15733149
- Volume :
- 20
- Database :
- OpenAIRE
- Journal :
- International Journal of Peptide Research and Therapeutics
- Accession number :
- edsair.doi...........641df177be35308592fc0712a319734a