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Antibiofilm properties of cathelicidin LL-37: an in-depth review
World Journal of Microbiology and Biotechnology, 2023Notwithstanding ceaseless endeavors toward developing effective antibiofilm chemotherapeutics, biofilm-associated infections continue to be one of the most perplexing challenges confronting medicine today. Endogenous host defense peptides, such as the human cathelicidin LL-37, are being propounded as promising options for treating such infectious ...
Hamed Memariani, Mojtaba Memariani
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Inactivation of the antimicrobial peptide LL-37 by pathogenic Leptospira
Microbial Pathogenesis, 2021Leptospires are aerobic, Gram-negative spirochetes with a high invasive capacity. Pathogenic leptospires secrete proteases that inactivate a variety of host's proteins including molecules of the extracellular matrix and of the human complement system. This strategy, used by several pathogens of medical importance, contributes to bacterial invasion and ...
Priscila N. Oliveira +8 more
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The role of the multifunctional peptide LL-37 in host defense
Frontiers in Bioscience, 2008Neutrophil granules contain several antimicrobial peptides (AMPs) that are important effector molecules of innate immunity. In mammals, the main families of these peptides are the cathelicidins and defensins. Several defensins have been characterized in humans, while there is only one human cathelicidin, designated LL-37.
Ylva, Kai-Larsen, Birgitta, Agerberth
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Circulating LL‐37 is a biomarker for eczema severity in children
Journal of the European Academy of Dermatology and Venereology, 2011AbstractBackground Eczema lesions are characterized by impaired expression of antimicrobial peptides such as cathelicidin, which play crucial roles in the innate immune defence against cutaneous infections. LL‐37 corresponds to amino acids 134–170 of human cathelicidin and is a multifunctional host defence molecule essential for normal immune ...
T F, Leung +5 more
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Salivary concentration of the antimicrobial peptide LL-37 in children
Archives of Oral Biology, 2012Antimicrobial peptides are important components of innate immunity, especially in the unique environment of the oral cavity. Lack of the human cathelicidin LL-37 has been implicated in severe periodontitis, whilst high salivary levels of LL-37 seem to increase caries resistance.
Sotiria, Davidopoulou +3 more
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Low serum levels of cathelicidin LL-37 in leprosy
Acta Tropica, 2011The antimicrobial peptide cathelicidin LL-37 possesses antituberculous activity, its association with other mycobacterial diseases, such as leprosy, is unknown. We studied serum cathelicidin and 25OH-vitamin D3 levels in 29 leprosy patients and 19 healthy individuals from Yemen.
Michael, Matzner +7 more
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Preparation of LL-37-Grafted Titanium Surfaces with Bactericidal Activity
Bioconjugate Chemistry, 2006Modification of material surfaces aimed at bestowing them with antimicrobial properties is a promising approach in the development of new biomaterials. Antimicrobial peptides (AMPs) are an attractive alternative to conventional antibiotics because of lack of toxicity, inherently high selectivity, and absence of immune response.
Gabriel, M.O. +4 more
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Assays for Identifying Inducers of the Antimicrobial Peptide LL-37
2016One promising approach to meet the growing problem of antibiotic resistance is to modulate host defense mechanisms, i.e., host-directed therapy (HDT), in the fight against infections. Induction of endogenous antimicrobial peptides (AMPs) via small molecular compounds, such as 1,25-dihydroxyvitamin D3 or phenylbutyrate, could provide one such HDT-based ...
Frank, Nylén +3 more
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Human Cathelicidin LL-37 Prevents Bacterial Biofilm Formation
Future Medicinal Chemistry, 2012Human pathogens often colonize their host by the formation of biofilms. These surface-attached aggregates of bacteria are characterized by a self-produced extracellular matrix, which makes them highly resistant towards antibiotic treatment. Their abilities to adhere to abiotic surfaces (e.g., catheters and other medical devices) also makes bacterial ...
Skovgård Jacobsen , Andreas +1 more
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ChemInform Abstract: The Chemistry and Biology of LL‐37
ChemInform, 2010AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Matthew F. Burton, Patrick G. Steel
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