Academic literature on the topic 'Peptide LL-37'
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Journal articles on the topic "Peptide LL-37"
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Nagant, C., B. Pitts, K. Nazmi, M. Vandenbranden, J. G. Bolscher, P. S. Stewart, and J. P. Dehaye. "Identification of Peptides Derived from the Human Antimicrobial Peptide LL-37 Active against Biofilms Formed by Pseudomonas aeruginosa Using a Library of Truncated Fragments." Antimicrobial Agents and Chemotherapy 56, no. 11 (August 20, 2012): 5698–708. http://dx.doi.org/10.1128/aac.00918-12.
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ABSTRACTPersistentPseudomonas aeruginosainfections are a major cause of morbidity and mortality in cystic fibrosis (CF) patients and are linked to the formation of a biofilm. The development of new biofilm inhibition strategies is thus a major challenge. LL-37 is the only human antimicrobial peptide derived from cathelicidin. The effects on theP. aeruginosaPAO1 strain of synthetic truncated fragments of this peptide were compared with the effects of the original peptide. Fragments of LL-37 composed of 19 residues (LL-19, LL13-31, and LL7-25) inhibited biofilm formation. The strongest antibiofilm activity was observed with the peptides LL7-37 and LL-31, which decreased the percentage of biomass formation at a very low concentration. Some peptides were also active on the bacteria within an established biofilm. LL7-31, LL-31, and LL7-37 increased the uptake of propidium iodide (PI) by sessile bacteria. The peptide LL7-37 decreased the height of the biofilm and partly disrupted it. The peptides active within the biofilm had an infrared spectrum compatible with an α-helix. LL-37, but not the peptides LL7-31 and LL7-37, showed cellular toxicity by permeabilizing the eukaryotic plasma membrane (uptake of ethidium bromide and release of lactate dehydrogenase [LDH]). None of the tested peptides affected mitochondrial activity in eukaryotic cells. In conclusion, a 25-amino-acid peptide (LL7-31) displayed both strong antimicrobial and antibiofilm activities. The peptide was even active on cells within a preformed biofilm and had reduced toxicity toward eukaryotic cells. Our results also suggest the contribution of secondary structures (α-helix) to the activity of the peptides on biofilms.
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Sieprawska-Lupa, Magdalena, Piotr Mydel, Katarzyna Krawczyk, Kinga Wójcik, Magdalena Puklo, Boguslaw Lupa, Piotr Suder, et al. "Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases." Antimicrobial Agents and Chemotherapy 48, no. 12 (December 2004): 4673–79. http://dx.doi.org/10.1128/aac.48.12.4673-4679.2004.
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ABSTRACT Cathelicidin LL-37 is one of the few human bactericidal peptides with potent antistaphylococcal activity. In this study we examined the susceptibility of LL-37 to proteolytic degradation by two major proteinases produced by Staphylococcus aureus, a metalloproteinase (aureolysin) and a glutamylendopeptidase (V8 protease). We found that aureolysin cleaved and inactivated LL-37 in a time- and concentration-dependent manner. Analysis of the generated fragments by mass spectroscopy revealed that the initial cleavage of LL-37 by aureolysin occurred between the Arg19-Ile20, Arg23-Ile24, and Leu31-Val32 peptide bonds, instantly annihilating the antibacterial activity of LL-37. In contrast, the V8 proteinase hydrolyzed efficiently only the Glu16-Phe17 peptide bond, rendering the C-terminal fragment refractory to further degradation. This fragment (termed LL-17-37) displayed antibacterial activity against S. aureus at a molar level similar to that of the full-length LL-37 peptide, indicating that the antibacterial activity of LL-37 resides in the C-terminal region. In keeping with LL-37 degradation by aureolysin, S. aureus strains that produce significant amounts of this metalloprotease were found to be less susceptible to LL-17-37 than strains expressing no aureolysin activity. Taken together, these data suggest that aureolysin production by S. aureus contributes to the resistance of this pathogen to the innate immune system of humans mediated by LL-37.
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Perez-Perez, David A., Teresa de J. Villanueva-Ramirez, Adriana E. Hernandez-Pedraza, Nestor G. Casillas-Vega, Patricia Gonzalez-Barranco, and Xristo Zarate. "The Small Metal-Binding Protein SmbP Simplifies the Recombinant Expression and Purification of the Antimicrobial Peptide LL-37." Antibiotics 10, no. 10 (October 19, 2021): 1271. http://dx.doi.org/10.3390/antibiotics10101271.
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(1) Background: The cathelicidin peptide LL-37 is a prominent molecule with many biological activities, including antimicrobial. Due to its importance, here, we describe the production of LL-37 tagged with SmbP, a relatively new carrier protein that improves the production of recombinant proteins and peptides in Escherichia coli. We present an alternative method for the rapid expression, purification, and antimicrobial evaluation of LL-37, that involves only one purification step. (2) Methods: A DNA construct of SmbP_LL-37 was transformed into E. coli BL21(DE3); after overnight expression, the protein was purified directly from the cell lysate using immobilized metal-affinity chromatography. SmbP_LL-37 was treated with Enterokinase to obtain the free LL-37 peptide. The antimicrobial activity of both SmbP_LL-37 and free LL-37 was determined using the colony forming unit assay method. (3) Results: SmbP_LL-37 was observed in the soluble fraction of the cell lysate; after purification with IMAC, protein gel electrophoresis, and analysis by ImageJ, it showed 90% purity. A total of 3.6 mg of SmbP_LL-37 was produced from one liter of cell culture. SmbP_LL-37 and free LL-37 both showed inhibition activity against Staphylococcus aureus and Escherichia coli. (4) Conclusions: The SmbP fusion protein is a valuable tool for producing biologically-active LL-37 peptide. The production method described here should be of interest for the expression and purification of additional cationic peptides, since it cuts the purification time considerably prior to determination of antimicrobial activity.
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Sigurdardottir, Thorgerdur, Pia Andersson, Mina Davoudi, Martin Malmsten, Artur Schmidtchen, and Mikael Bodelsson. "In Silico Identification and Biological Evaluation of Antimicrobial Peptides Based on Human Cathelicidin LL-37." Antimicrobial Agents and Chemotherapy 50, no. 9 (September 2006): 2983–89. http://dx.doi.org/10.1128/aac.01583-05.
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ABSTRACT Bacterial lipopolysaccharides (LPS) are important triggers of the widespread inflammatory response, which contributes to the development of multiple organ failure during sepsis. The helical 37-amino-acid-long human antimicrobial peptide LL-37 not only possesses a broad-spectrum antimicrobial activity but also binds and neutralizes LPS. However, the use of LL-37 in sepsis treatment is hampered by the fact that it is also cytotoxic. To find a less toxic analog of LL-37, we used in silico analysis to identify amphipathic helical regions of LL-37. A 21-amino-acid fragment (GKE) was synthesized, the biological actions of which were compared to those of two equally long peptides derived from the N and C termini of LL-37 as well as native LL-37. GKE displayed antimicrobial activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Candida albicans, and Candida parapsilosis that was similar to or even stronger than LL-37. GKE, as well as the equally long control peptides, attracted granulocytes in a fashion similar to that of LL-37, while only GKE was as potent as LL-37 in inhibiting LPS-induced vascular nitric oxide production. GKE caused less hemolysis and apoptosis in human cultured smooth muscle cells than LL-37. In summary, we have identified an active domain of LL-37, GKE, which displays antimicrobial activity in vitro and LPS-binding activity similar to those of LL-37 but is less toxic. GKE therefore holds promise as a template for the development of peptide antibiotics for the treatment of sepsis.
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Yang, De, Qian Chen, Albert P. Schmidt, G. Mark Anderson, Ji Ming Wang, Joseph Wooters, Joost J. Oppenheim, and Oleg Chertov. "Ll-37, the Neutrophil Granule–And Epithelial Cell–Derived Cathelicidin, Utilizes Formyl Peptide Receptor–Like 1 (Fprl1) as a Receptor to Chemoattract Human Peripheral Blood Neutrophils, Monocytes, and T Cells." Journal of Experimental Medicine 192, no. 7 (October 2, 2000): 1069–74. http://dx.doi.org/10.1084/jem.192.7.1069.
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We have previously shown that antimicrobial peptides like defensins have the capacity to mobilize leukocytes in host defense. LL-37 is the cleaved antimicrobial 37-residue, COOH-terminal peptide of hCAP18 (human cationic antimicrobial protein with a molecular size of 18 kD), the only identified member in humans of a family of proteins called cathelicidins. LL-37/hCAP18 is produced by neutrophils and various epithelial cells. Here we report that LL-37 is chemotactic for, and can induce Ca2+ mobilization in, human monocytes and formyl peptide receptor–like 1 (FPRL1)-transfected human embryonic kidney 293 cells. LL-37–induced Ca2+ mobilization in monocytes can also be cross-desensitized by an FPRL1-specific agonist. Furthermore, LL-37 is also chemotactic for human neutrophils and T lymphocytes that are known to express FPRL1. Our results suggest that, in addition to its microbicidal activity, LL-37 may contribute to innate and adaptive immunity by recruiting neutrophils, monocytes, and T cells to sites of microbial invasion by interacting with FPRL1.
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Rinker, Sherri D., Michael P. Trombley, Xiaoping Gu, Kate R. Fortney, and Margaret E. Bauer. "Deletion ofmtrCin Haemophilus ducreyi Increases Sensitivity to Human Antimicrobial Peptides and Activates the CpxRA Regulon." Infection and Immunity 79, no. 6 (March 28, 2011): 2324–34. http://dx.doi.org/10.1128/iai.01316-10.
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ABSTRACTHaemophilus ducreyiresists killing by antimicrobial peptides encountered during human infection, including cathelicidin LL-37, α-defensins, and β-defensins. In this study, we examined the role of the proton motive force-dependent multiple transferable resistance (MTR) transporter in antimicrobial peptide resistance inH. ducreyi. We found a proton motive force-dependent effect onH. ducreyi's resistance to LL-37 and β-defensin HBD-3, but not α-defensin HNP-2. Deletion of the membrane fusion protein MtrC renderedH. ducreyimore sensitive to LL-37 and human β-defensins but had relatively little effect on α-defensin resistance. ThemtrCmutant 35000HPmtrCexhibited phenotypic changes in outer membrane protein profiles, colony morphology, and serum sensitivity, which were restored to wild type bytrans-complementation withmtrC. Similar phenotypes were reported in acpxAmutant; activation of the two-component CpxRA regulator was confirmed by showing transcriptional effects on CpxRA-regulated genes in 35000HPmtrC. AcpxRmutant had wild-type levels of antimicrobial peptide resistance; acpxAmutation had little effect on defensin resistance but led to increased sensitivity to LL-37. 35000HPmtrCwas more sensitive than thecpxAmutant to LL-37, indicating that MTR contributed to LL-37 resistance independent of the CpxRA regulon. The CpxRA regulon did not affect proton motive force-dependent antimicrobial peptide resistance; however, 35000HPmtrChad lost proton motive force-dependent peptide resistance, suggesting that the MTR transporter promotes proton motive force-dependent resistance to LL-37 and human β-defensins. This is the first report of a β-defensin resistance mechanism inH. ducreyiand shows that LL-37 resistance inH. ducreyiis multifactorial.
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Zhang, Yingxia, Jayaram Lakshmaiah Narayana, Qianhui Wu, Xiangli Dang, and Guangshun Wang. "Structure and Activity of a Selective Antibiofilm Peptide SK-24 Derived from the NMR Structure of Human Cathelicidin LL-37." Pharmaceuticals 14, no. 12 (November 30, 2021): 1245. http://dx.doi.org/10.3390/ph14121245.
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The deployment of the innate immune system in humans is essential to protect us from infection. Human cathelicidin LL-37 is a linear host defense peptide with both antimicrobial and immune modulatory properties. Despite years of studies of numerous peptides, SK-24, corresponding to the long hydrophobic domain (residues 9–32) in the anionic lipid-bound NMR structure of LL-37, has not been investigated. This study reports the structure and activity of SK-24. Interestingly, SK-24 is entirely helical (~100%) in phosphate buffer (PBS), more than LL-37 (84%), GI-20 (75%), and GF-17 (33%), while RI-10 and 17BIPHE2 are essentially randomly coiled (helix%: 7–10%). These results imply an important role for the additional N-terminal amino acids (likely E16) of SK-24 in stabilizing the helical conformation in PBS. It is proposed herein that SK-24 contains the minimal sequence for effective oligomerization of LL-37. Superior to LL-37 and RI-10, SK-24 shows an antimicrobial activity spectrum comparable to the major antimicrobial peptides GF-17 and GI-20 by targeting bacterial membranes and forming a helical conformation. Like the engineered peptide 17BIPHE2, SK-24 has a stronger antibiofilm activity than LL-37, GI-20, and GF-17. Nevertheless, SK-24 is least hemolytic at 200 µM compared with LL-37 and its other peptides investigated herein. Combined, these results enabled us to appreciate the elegance of the long amphipathic helix SK-24 nature deploys within LL-37 for human antimicrobial defense. SK-24 may be a useful template of therapeutic potential.
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Yason, John Anthony, Sitara Swarna Rao Ajjampur, and Kevin Shyong Wei Tan. "Blastocystis Isolate B Exhibits Multiple Modes of Resistance against Antimicrobial Peptide LL-37." Infection and Immunity 84, no. 8 (May 23, 2016): 2220–32. http://dx.doi.org/10.1128/iai.00339-16.
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Blastocystisis one of the most common eukaryotic organisms found in humans and many types of animals. Several reports have identified its role in gastrointestinal disorders, although its pathogenicity is yet to be clarified.Blastocystisis transmitted via the fecal-to-oral route and colonizes the large intestines. Epithelial cells lining the intestine secrete antimicrobial peptides (AMPs), including beta-defensins and cathelicidin, as a response to infection. This study explores the effects of host colonic antimicrobial peptides, particularly LL-37, a fragment of cathelicidin, on differentBlastocystissubtypes.Blastocystisis composed of several subtypes that have genetic, metabolic, and biological differences. These subtypes also have various outcomes in terms of drug treatment and immune response. In this study,Blastocystisisolates from three different subtypes were found to induce intestinal epithelial cells to secrete LL-37. We also show that among the antimicrobial peptides tested, only LL-37 has broad activity on all the subtypes. LL-37 causes membrane disruption and causesBlastocystisto change shape.Blastocystissubtype 7 (ST7), however, showed relative resistance to LL-37. An isolate, ST7 isolate B (ST7-B), from this subtype releases proteases that can degrade the peptide. It also makes the environment acidic, which causes attenuation of LL-37 activity. TheBlastocystisST7-B isolate was also observed to have a thicker surface coat, which may protect the parasite from direct killing by LL-37. This study determined the effects of LL-37 on differentBlastocystisisolates and indicates that AMPs have significant roles inBlastocystisinfections.
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Amagai, Ryo, Toshiya Takahashi, Hitoshi Terui, Taku Fujimura, Kenshi Yamasaki, Setsuya Aiba, and Yoshihide Asano. "The Antimicrobial Peptide Cathelicidin Exerts Immunomodulatory Effects via Scavenger Receptors." International Journal of Molecular Sciences 24, no. 1 (January 3, 2023): 875. http://dx.doi.org/10.3390/ijms24010875.
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An active form of cathelicidin antimicrobial peptide, LL-37, has immunomodulatory and stimulatory effects, though the specific pathways are not clear. The purpose of this study was to identify the cellular pathways by which LL-37 amplifies the inflammation induced by damage-associated molecular patterns (DAMPs). We performed DNA microarray, reverse transcription polymerase chain reaction, immunoblotting, and proximity ligation assays using cultured keratinocytes treated with LL-37 and/or the DAMP poly(I:C), a synthetic double-stranded RNA. In contrast to the combination of LL-37 and poly(I:C), LL-37 alone induced genes related to biological metabolic processes such as VEGFA and PTGS2 (COX-2). Inhibition of FPR2, a known receptor for cathelicidin, partially suppressed the induction of VEGFA and PTGS2. Importantly, VEGFA and PTGS2 induced by LL-37 alone were diminished by the knockdown of scavenger receptors including SCARB1 (SR-B1), OLR1 (SR-E1), and AGER (SR-J1). Moreover, LL-37 alone, as well as the combination of LL-37 and poly(I:C), showed proximity to the scavenger receptors, indicating that LL-37 acts via scavenger receptors and intermediates between them and poly(I:C). These results showed that the broad function of cathelicidin is generally dependent on scavenger receptors. Therefore, inhibitors of scavenger receptors or non-functional mock cathelicidin peptides may serve as new anti-inflammatory and immunosuppressive agents.
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Mirzaee, Malihe, Edita Holásková, Alžbeta Mičúchová, David J. Kopečný, Zhila Osmani, and Ivo Frébort. "Long-Lasting Stable Expression of Human LL-37 Antimicrobial Peptide in Transgenic Barley Plants." Antibiotics 10, no. 8 (July 23, 2021): 898. http://dx.doi.org/10.3390/antibiotics10080898.
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Antimicrobial peptides play a crucial role in the innate immune system of multicellular organisms. LL-37 is the only known member of the human cathelicidin family. As well as possessing antibacterial properties, it is actively involved in various physiological responses in eukaryotic cells. Accordingly, there is considerable interest in large-scale, low-cost, and microbial endotoxin-free production of LL-37 recombinant peptides for pharmaceutical applications. As a heterologous expression biofactory, we have previously obtained homologous barley (Hordeum vulgare L.) as an attractive vehicle for producing recombinant human LL-37 in the grain storage compartment, endosperm. The long-term stability of expression and inheritance of transgenes is necessary for the successful commercialization of recombinant proteins. Here, we report the stable inheritance and expression of the LL-37 gene in barley after six generations, including two consecutive seasons of experimental field cultivation. The transgenic plants showed normal growth and remained fertile. Based on the bacteria viability test, the produced peptide LL-37 retained high antibacterial activity.
Dissertations / Theses on the topic "Peptide LL-37"
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El, Abbouni Sarah. "Microencapsulation of LL-37 Antimicrobial Peptide in PLGA." Digital WPI, 2016. https://digitalcommons.wpi.edu/etd-theses/235.
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Antimicrobial peptides are key actors in organisms€™ immune systems. They play an important role in phagocytosis, breaking bacteria membranes. They destroy the microbes, keeping them from repairing themselves, and therefore do not promote antimicrobial resistance. LL37 is a peptide produced by the human body. It is a short amino acid chain that is particularly active on the skin and mucous membranes. It has antimicrobial and fungal activity as well as wound healing properties, which makes it a very interesting active substance in wound treatment. However, its fragile and sensitive structure is a challenge to its use. Nowadays, encapsulation in a biocompatible polymer system is a promising technique in drug delivery, and presents a solution to LL37 administration and delivery. LL37 is a hydrophilic active substance, it will be trapped in PLGA (poly (lactic-co-glycolic acid)) by double emulsion and the microspheres will be shaped and stabilized by solvent evaporation. The capsules will be characterized by Dynamic Light Scattering (DLS) and Scanning Electron Microscopy. Their main features, drug loading, encapsulation efficiency and release profile, are determined using the Bradford assay. Since the peptide is expensive and delicate, it is important to optimize its encapsulation. For that reason, we will adapt the process to have the best drug loading as possible using water in oil in oil emulsions. For an external use, the capsules would be used over a few days, so having a fast release is very relevant. The larger the specific surface area, the faster the diffusion. For that reason, we will also study the impact of porosity on the release profile. As a result, different types of capsules will be synthesized, with higher porosity and by two processes: aqueous double emulsion and oil double emulsion. Their characteristic features and impact on bacterial pathogens will be determined and compared in order to determine their optimal synthesis process and formulation in given conditions of use.
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Dannehl, Claudia. "Fragments of the human antimicrobial LL-37 and their interaction with model membranes." Phd thesis, Universität Potsdam, 2013. http://opus.kobv.de/ubp/volltexte/2013/6814/.
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A detailed description of the characteristics of antimicrobial peptides (AMPs) is highly demanded, since the resistance against traditional antibiotics is an emerging problem in medicine. They are part of the innate immune system in every organism, and they are very efficient in the protection against bacteria, viruses, fungi and even cancer cells. Their advantage is that their target is the cell membrane, in contrast to antibiotics which disturb the metabolism of the respective cell type. This allows AMPs to be more active and faster. The lack of an efficient therapy for some cancer types and the evolvement of resistance against existing antitumor agents make AMPs promising in cancer therapy besides being an alternative to traditional antibiotics.
The aim of this work was the physical-chemical characterization of two fragments of LL-37, a human antimicrobial peptide from the cathelicidin family. The fragments LL-32 and LL-20 exhibited contrary behavior in biological experiments concerning their activity against bacterial cells, human cells and human cancer cells. LL-32 had even a higher activity than LL-37, while LL-20 had almost no effect. The interaction of the two fragments with model membranes was systematically studied in this work to understand their mode of action. Planar lipid films were mainly applied as model systems in combination with IR-spectroscopy and X-ray scattering methods. Circular Dichroism spectroscopy in bulk systems completed the results.
In the first approach, the structure of the peptides was determined in aqueous solution and compared to the structure of the peptides at the air/water interface. In bulk, both peptides are in an unstructured conformation. Adsorbed and confined to at the air-water interface, the peptides differ drastically in their surface activity as well as in the secondary structure. While LL-32 transforms into an α-helix lying flat at the water surface, LL-20 stays partly unstructured. This is in good agreement with the high antimicrobial activity of LL-32.
In the second approach, experiments with lipid monolayers as biomimetic models for the cell membrane were performed. It could be shown that the peptides fluidize condensed monolayers of negatively charged DPPG which can be related to the thinning of a bacterial cell membrane. An interaction of the peptides with zwitterionic PCs, as models for mammalian cells, was not clearly observed, even though LL-32 is haemolytic.
In the third approach, the lipid monolayers were more adapted to the composition of human erythrocyte membranes by incorporating sphingomyelin (SM) into the PC monolayers. Physical-chemical properties of the lipid films were determined and the influence of the peptides on them was studied. It could be shown that the interaction of the more active LL-32 is strongly increased for heterogeneous lipid films containing both gel and fluid phases, while the interaction of LL-20 with the monolayers was unaffected. The results indicate an interaction of LL-32 with the membrane in a detergent-like way.
Additionally, the modelling of the peptide interaction with cancer cells was performed by incorporating some negatively charged lipids into the PC/SM monolayers, but the increased charge had no effect on the interaction of LL-32. It was concluded, that the high anti-cancer activity of the peptide originates from the changed fluidity of cell membrane rather than from the increased surface charge. Furthermore, similarities to the physical-chemical properties of melittin, an AMP from the bee venom, were demonstrated.Aufgrund der steigenden Resistenzen von Zellstämmen gegen traditionelle Therapeutika sind alternative medizinische Behandlungsmöglichkeiten für bakterielle Infektionen und Krebs stark gefragt. Antimikrobielle Peptide (AMPs) sind Bestandteil der unspezifischen Immunabwehr und kommen in jedem Organismus vor. AMPs lagern sich von außen an die Zellmembran an und zerstören ihre Integrität. Das macht sie effizient und vor allem schnell in der Wirkung gegen Bakterien, Viren, Pilzen und sogar Krebszellen. Das Ziel dieser Arbeit lag in der physikalisch-chemischen Charakterisierung zweier Peptidfragmente die unterschiedliche biologische Aktivität aufweisen. Die Peptide LL-32 und LL-20 waren Teile des humanen LL-37 aus der Kathelizidin-Familie. LL-32 wies eine stärke Aktivität als das Mutterpeptid auf, während LL-20 kaum aktiv gegen die verschiedenen Zelltypen war. In dieser Arbeit wurde die Wechselwirkung der Peptide mit Zellmembranen systematisch anhand von zweidimensionalen Modellmembranen in dieser Arbeit untersucht. Dafür wurden Filmwaagenmessungen mit IR-spektroskopischen und Röntgenstreumethoden gekoppelt. Circulardichroismus-Spektroskopie im Volumen komplementierte die Ergebnisse. In der ersten Näherung wurde die Struktur der Peptide in Lösung mit der Struktur an der Wasser/Luft-Grenzfläche verglichen. In wässriger Lösung sind beide Peptidfragmente unstrukturiert, nehmen jedoch eine α-helikale Sekundärstruktur an, wenn sie an die Wasser/Luft-Grenzfläche adsorbiert sind. Das biologisch unwirksamere LL-20 bleibt dabei teilweise ungeordnet. Das steht im Zusammenhang mit einer geringeren Grenzflächenaktivität des Peptids. In der Zweiten Näherung wurden Versuche mit Lipidmonoschichten als biomimetisches Modell für die Wechselwirkung mit der Zellmembran durchgeführt. Es konnte gezeigt werden, dass sich die Peptide fluidisierend auf negativ geladene Dipalmitylphosphatidylglycerol (DPPG) Monoschichten auswirken, was einer Membranverdünnung an Bakterienzellen entspricht. Eine Interaktion der Peptide mit zwitterionischem Phosphatidylcholin (PC), das als Modell für Säugetierzellen verwendet wurde, konnte nicht klar beobachtet werden, obwohl biologische Experimente das hämolytische Verhalten zumindest von LL-32 zeigten. In der dritten Näherung wurde das Membranmodell näher an die Membran von humanen Erythrozyten angepasst, indem gemischte Monoschichten aus Sphingomyelin (SM) und PC hergestellt wurden. Die physikalisch-chemischen Eigenschaften der Lipidfilme wurden zunächst ausgearbeitet und anschließend der Einfluss der Peptide untersucht. Es konnte anhand verschiedener Versuche gezeigt werden, dass die Wechselwirkung von LL-32 mit der Modellmembran verstärkt ist, wenn eine Koexistenz von fluiden und Gelphasen auftritt. Zusätzlich wurde die Wechselwirkung der Peptide mit der Membran von Krebszellen imitiert, indem ein geringer Anteil negativ geladener Lipide in die Monoschicht eingebaut wurde. Das hatte allerdings keinen nachweislichen Effekt, so dass geschlussfolgert werden konnte, dass die hohe Aktivität von LL-32 gegen Krebszellen ihren Grund in der veränderten Fluidität der Membran hat und nicht in der veränderten Oberflächenladung. Darüber hinaus wurden Ähnlichkeiten zu Melittin, einem AMP aus dem Bienengift, dargelegt. Die Ergebnisse dieser Arbeit sprechen für einen Detergenzien-artigen Wirkmechanismus des Peptids LL-32 an der Zellmembran.
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Filewod, Niall Christopher Jack. "Immunomodulatory effects of LL-37 in the epithelia." Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/927.
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The cationic host defence peptide LL-37 is an immunomodulatory agent that plays an important role in epithelial innate immunity. Previously, concentrations of LL-37 thought to represent levels present during inflammation have been shown to elicit the production of cytokines and chemokines by epithelial cells. To investigate the potential of lower concentrations of LL-37 to alter epithelial cell responses, normal primary keratinocytes and bronchial epithelial cells were treated with pro-inflammatory stimuli in the presence or absence of 1 – 3 μg/ml LL-37. Low, physiologically relevant concentrations of LL-37 synergistically increased IL-8 production by both proliferating and differentiated keratinocytes in response to IL-1β and the TLR5 agonist flagellin, and synergistically increased IL-8 production by bronchial epithelial cells in response to IL-1β, flagellin, and the TLR2/1 agonist PAM3CSK4. Treatment of bronchial epithelial cells with LL-37 and the TLR3 agonist poly(I:C) resulted in synergistic increases in IL-8 release and cytotoxicity. The synergistic increase in IL-8 production observed when keratinocytes were co-stimulated with flagellin and LL-37 was suppressed by pretreatment with inhibitors of Src-family kinase signalling and NF-κB translocation. These data suggest that low concentrations of LL-37 may alter epithelial responses to microbes in vivo. Microarray analysis of keratinocyte transcriptional responses after LL-37 treatment suggest that LL-37 may alter the expression of growth factors and a number of genes important to innate immune responses. LL-37 may thus play a more important role than previously suspected in the regulation of epithelial inflammation; an improved understanding of the mechanisms by which LL-37 alters chemokine responses could lead to the development of novel anti-infective and anti-inflammatory therapeutics.
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Li, Yue Xin. "The human cationic host defense peptide LL-37 modulates neutrophil apoptosis and chemokine responses." Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/31726.
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LL-37 is a human cationic peptide expressed primarily by neutrophils and epithelial cells.
It is a 37 amino acid peptide that belongs to the cathelicidin family of the cationic host defense
peptides. Accumulating evidence has demonstrated that LL-37 has multiple immunomodulatory
properties. The modulatory effects of LL-37 on neutrophils were investigated here, and LL-37
was shown to be a potent inhibitor of spontaneous apoptosis in human neutrophils, signalling
through P2X₇ receptors and G-protein-coupled receptors other than the formyl peptide receptor-like-
1 molecule. Inhibition of neutrophil apoptosis involved modulation of Mcl-1 expression,
inhibition of BID and procaspase-3 cleavage, and the activation of phosphatidylinositol-3 kinase
and protein kinase C but not the extracellular signal-regulated kinase 1/2 mitogen-activated
protein kinase (ERK1/2) pathway. In addition, LL-37 modified neutrophil cytokine/chemokine
responses to pro-inflammatory stimuli in a stimulus-specific manner. Specifically, LL-37
abrogated LPS-induced TNF-a cytokine production while enhancing IL-1β elicited release of
TNF-a as well as a number of chemokines including IL-8, Gro-a, CCL-22 and Mip-la . The
increased release of chemokines induced synergistically by LL-37 and IL-1β resulted from de
novo protein synthesis and was found to be associated with the signalling through the ERK1/2
and p38 MAP kinases and nuclear factor κΒ pathways. These novel immunomodulatory
properties of LL-37 may contribute to peptide-mediated enhancement of innate host defenses
against acute infection and are of considerable significance in the development of such peptides
and their synthetic analogs as potential therapeutics for use against multiple antibiotic-resistant
infectious diseases.Science, Faculty of
Microbiology and Immunology, Department of
Graduate
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Zhang, P. "Identification of staphylococcal genes involved in resistance to the human antimicrobial peptide LL-37." Thesis, University College London (University of London), 2012. http://discovery.ucl.ac.uk/1380282/.
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Staphylococcus aureus is well-known for its ability to acquire resistance to a broad range of antimicrobial agents and a limited number of commercially available antibiotics exist that are active against multidrug resistant strains. Antimicrobial peptides have been suggested as promising alternatives to current antimicrobials due to their potent antimicrobial activity against a broad range of microorganisms including multidrug resistant bacteria, and a membrane-lytic mode of action that is thought to have low possibility of inducing bacterial resistance. This study describes the identification of S. aureus genes involved in resistance to the human cationic antimicrobial peptide LL-37, with a particular interest in the effects of a physiological concentration of bicarbonate on the resistance mechanism. Transposon mutagenesis and recombinase-based in vivo expression technology systems were designed to enable genome-wide screening. A S. aureus transposon mutant library was screened for increased resistance to LL-37 in the presence of bicarbonate. Mutants with insertions in yycH and yycI, demonstrated bicarbonate-dependent resistance to LL-37. Both yycH and yycI form part of a predicted operon yycFGHI in S. aureus, and have been shown to be suppressors of an essential two component system YycFG in B. subtilis that regulates cell wall metabolism. The resistance of S. aureus small colony variants (SCVs) to LL-37 was also investigated. SCVs defective in hemB, menD or aroD, demonstrated bicarbonate-dependent resistance to LL-37. Furthermore, SigB (a global regulator) and TcaR (an activator of protein A) were found to exert opposite effects on resistance to LL-37 in the presence of bicarbonate. Strains defective in TcaR showed bicarbonate-dependent resistance to LL-37, interestingly, this resistance was abolished by either deleting sigB or repairing tcaR in these strains. These data suggest that YycFG, SigB, TcaR and the SCV phenotype may play important roles in resistance to LL-37 under in vivo conditions where bicarbonate is present.
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Milhan, Noala Vicensoto Moreira [UNESP]. "Avaliação do peptídeo LL-37 em contato com células-tronco da polpa dentária." Universidade Estadual Paulista (UNESP), 2017. http://hdl.handle.net/11449/149791.
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
O peptídeo LL-37 (catelicidina derivada de humano), é liberado por algumas células humanas e capaz de neutralizar os tecidos com lipopolissacarídeo (LPS), além de atrair células da polpa, e induzir a angiogênese, características que o tornam um possível adjunto para a regeneração do complexo dentino-pulpar. O objetivo desse trabalho foi avaliar in vitro a biocompatibilidade do peptídeo LL-37 nas concentrações de 5 e 10 μg/mL, e sua possível atuação na diferenciação de células-tronco da polpa dentária (DPSC) para odontoblastos- like. Com esse propósito, foram avaliados: (a) a citotoxicidade, pelo teste MTT; (b) a genotoxicidade, através do ensaio do micronúcleo; (c) a produção e quantificação de óxido nítrico; (d) as fases do ciclo celular, por citometria; (e) a expressão de alguns genes associados à formação de tecido mineralizado, através do teste qRT-PCR; (f) o conteúdo de proteína total; (g) a atividade de fosfatase alcalina (ALP); e (h) a produção de sialofosfoproteína dentinária (DSPP), pelo ensaio imunoenzimático ELISA. Foi observado que as concentrações de 5 e 10 μg/mL de LL-37 não foram citotóxicas e ainda aumentaram, em geral, a viabilidade celular (p<0,05), sendo que os maiores valores de absorbância foram observados no 3° dia de contato. As concentrações testadas também não induziram genotoxicidade, após 7 dias de contato, tendo sido genotóxico apenas o grupo controle positivo (EMS) (p<0,05). Ainda, não foi observado diferença estatisticamente significativa na produção de nitrito, pelas células expostas ao LL-37 após 7 dias, em ambas as concentrações. A análise do ciclo celular, evidenciou maior porcentual de células na fase G0/G1, em todos os grupos (p<0,05). Quando estes foram comparados, foi observado maior quantidade de células na fase G0/G1 na concentração de 10 μg/mL de LL- 37 comparada ao grupo controle (p<0,05). Por outro lado, o grupo controle exibiu mais células na fase G2 e em mitose (M) que os grupos tratados com 5 e 10 μg/mL de LL-37 (p<0,05), e mais células na interfase (S) que o grupo tratado com 10 μg/mL de LL-37 (p<0,05). A análise da expressão gênica demonstrou que não houve aumento de expressão dos genes fosfatase alcalina, osteocalcina, osteopontina e Runx2 após tratamento com ambas as concentrações do peptídeo, no 3° dia. Além disso, não foi observado diferença estatisticamente significativa na ALP nos grupos tratados e controle, após 3 e 14 dias, enquanto o conteúdo de proteína total foi maior aos 14 dias nos grupos tratados com LL-37 (p<0,05). Ainda, aos 3 dias, a produção da proteína DSPP foi maior no grupo tratado com 10 μg/mL de LL-37 (p<0,05). Com base nesses resultados, pode-se concluir que o LL-37 é biocompatível nas concentrações testadas nesse trabalho, e ainda aumenta o número de células viáveis, principalmente em período inicial. Além disso, aos 3 dias, na concentração de 10 μg/mL, ele retarda o ciclo celular e aumenta a expressão da proteína DSPP, além de aumentar a síntese proteica aos 14 dias, o que indica que esse peptídeo pode desempenhar algum tipo de função na diferenciação odontoblástica.
The LL-37 peptide (human derived cathelicidin) is released by some human cells and able of neutralizing the tissues that present lipopolysaccharide (LPS), as well as, attracts pulp cells and induces angiogenesis; characteristics that makes it a possible adjunct for regeneration of the dentin-pulp complex. The aim of this study was evaluate in vitro the biocompatibility of LL-37 in the concentrations of 5 and 10 μg/mL, and its possible performance in the differentiation of dental pulp stem cells (DPSC) into odontoblasts-like cells. For this purpose, it was evaluated: (a) the cytotoxicity by MTT assay; (b) the genotoxicity by the micronucleus test; (c) the production and quantification of nitric oxide; (d) the cell cycle, by flow cytometry; (e) the expression of genes associated with the mineralization by qRT-PCR; (f) the total protein content; (g) the alkaline phosphatase activity (ALP); and (h) the production of dentine sialofosfoprotein (DSPP) by indirect enzyme-linked immunosorbent assay (ELISA). It was observed that the concentrations of 5 and 10 μg/ml of LL-37 were not cytotoxic, in addition to they increased, in general, the cell viability (p<0,05). Moreover, higher absorbance values were observed on 3rd day of contact. After 7 days, the tested concentrations also did not induce genotoxicity, (p<0,05); only the positive control group (EMS) was genotoxic (p<0.05). Furthermore, there was not statistical significance in the nitrite production by the cells exposed to LL-37 for 7 days, in both concentrations. The cell cycle test showed higher percentage of cells in the phase G0/G1 in all groups (p<0.05). When they were compared, it was noticied that concentration of 10 ug/ml of LL-37 arrested the cells in G0/G1 compared to the control group (p<0.05). On the other hand, the control group, exhibited higher amount of cells in G2 and mitosis (M) than the others (p<0.05) and also higher number of cells in interfase (S) than the group treated with 10 μg/mL of LL-37 (p<0.05). On the 3rd day, the analysis of gene expression demonstrated no increase in the expression of the genes alkaline phosphatase, osteocalcin, osteopontin and Runx2, after treatment with both peptide concentrations. Furthermore, it was not observed statistical significance in the ALP in the treated and control groups after 3 and 14 days, while total protein content was higher in the groups treated with LL-37, at 14 days (p<0.05). On the 3rd day, the production of DSPP protein was higher in the group treated with 10 μg/mL of LL-37 (p<0.05). Based on these results, it can be concluded that LL-37 is biocompatible at these concentrations and increases the number of viable cells, especially in the initial period. Moreover, on the 3rd day, the concentration of 10 μg/mL arrests the cell cycle, and increases the expression of DSPP protein, in addition to raising the protein content at 14 days, which indicates that this peptide may present some kind of function in the odontoblastic differentiation.
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Ghannad, Mona. "Design and Synthesis of Collagen-binding Anti-microbial Proteins." Thèse, Université d'Ottawa / University of Ottawa, 2011. http://hdl.handle.net/10393/19981.
Full textAbstract:
The Herpes simplex virus (HSV) is a virus that commonly infects the skin, and mucous membrane of the mouth, genitalia, and the eye. HSV-1 is the strain that is most commonly associated with corneal infections, and it is the most frequent cause of corneal blindness in North America [1]. Currently no cure is available, and many limitations are characterized by the currently available synthetic antiviral drugs, which suggest the need for other potential drug alternatives and delivery strategies. Anti-microbial peptides are naturally occurring peptides that are potent killers of a broad range of micro-organisms, including bacteria, fungi, and viruses [2]. AMPs are known to be a key component of the innate immune response at the human ocular surface. The human cathelicidin-derived AMP, LL-37, expressed in human corneal epithelial cells provides a wide range of protection against viral pathogens such as HSV-1 [3]. My thesis research addressed the design and recombinant production of hybrid AMP sequences containing LL-37 with the potential ability to form chemical or physical associations with a Collagen scaffold material, such as those used in current artificial cornea constructs to address the need for alternative anti-viral drugs. Three fusion proteins were tested, and compared for feasible design anti-microbial peptide expression and purification in E. coli. It was illustrated that the thioredoxin and SUMO fusion systems are good candidates for successful recombinant production of active designed peptides. The point-mutated LL-37 sequence was successfully expressed and purified using the thioredoxin fusion system. It was demonstrated that this modified LL-37 was effective against HSV-1 infection. The SUMO system was used to express the bio-functional LL-37 containing a collagen-binding sequence. Further work is required to address issues regarding recombinant AMP production, such as increasing enzymatic cleavage efficacy, and minimizing proteolytic degradation or modification.
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Li, Hsin-Ni. "Impact of cationic host defence peptide LL-37 on human neutrophil death and inflammatory responses." Thesis, University of Edinburgh, 2011. http://hdl.handle.net/1842/5597.
Full textAbstract:
Cathelicidins are cationic host defence peptides (CHDP) with essential roles in the innate defence system. These peptides have antimicrobial potential and the capacity to modulate innate immunity and inflammatory processes. Neutrophils (PMN) are the main reservoir of cathelicidins and play key roles in first line defence against infection. The appropriate regulation of PMN function, death, and clearance is critical to innate immunity, and the efferocytosis of apoptotic PMN, in contrast to necrotic cells, is proposed to promote the resolution of inflammation. In this thesis I demonstrate that the human cathelicidin LL-37 rapidly induced secondary necrosis of apoptotic human PMN and identify the essential C-terminal region of LL-37 required for this activity. In addition to the induction of secondary necrosis, higher concentrations of LL-37 also promoted PMN granule contents release. LL-37-induced secondary necrosis did not affect PMN ingestion by human monocyte-derived macrophages and, in contrast to expectation, was not proinflammatory. Interestingly, the anti-inflammatory effects of apoptotic PMN on activated macrophages were retained and even potentiated where LL-37-mediated secondary necrosis induced anti-inflammatory granule content release. Consistent with the results of in vitro studies, in vivo murine sterile peritonitis model revealed the same phenomenon: LL-37-induced secondary necrosis diminished inflammatory responses with decreased PMN influx. I also present data on LL-37- mediated modulation of innate immune effector cell cytokines responses to inflammatory signals. I propose that during acute inflammation LL-37 can modulate innate immune responses through its activity on cytokine production, and that LL-37-mediated secondary necrosis of apoptotic PMN has anti-inflammatory effects, but may also mediate host damage by promoting the release of potentially harmful intracellular contents under chronic or dysregulated conditions.
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Milhan, Noala Vicensoto Moreira. "Avaliação do peptideo LL-37 em contato com células-tronco da polpa dentária /." São José dos Campos, 2017. http://hdl.handle.net/11449/149791.
Full textAbstract:
Orientador: Samira Esteves Afonso CamargoBanca: Luana Marotta Reis de Vasconcellos
Banca: Mônica Ghislaine Oliveira Alves
Banca: Cristina Pacheco Soares
Banca: Cacio de Moura Netto
Resumo: O peptídeoLL-37 (catelicidina derivada de humano), é liberado por algumas células humanas e capaz de neutralizar os tecidos com lipopolissacarídeo (LPS), além de atrair células da polpa, e induzir a angiogênese, características que o tornam um possível adjunto para a regeneração do complexo dentino-pulpar. O objetivo desse trabalho foi avaliar in vitro a biocompatibilidade do peptídeo LL-37 nas concentrações de 5 e 10 µg/mL, e sua possível atuação na diferenciação de células-tronco da polpa dentária (DPSC) para odontoblastoslike. Com esse propósito, foram avaliados: (a) a citotoxicidade, pelo teste MTT; (b) a genotoxicidade, através do ensaio do micronúcleo; (c) a produção e quantificação de óxido nítrico; (d) as fases do ciclo celular, por citometria; (e) a expressão de alguns genes associados à formação de tecido mineralizado, através do teste qRT-PCR; (f) o conteúdo de proteína total; (g) a atividade de fosfatase alcalina (ALP); e (h) a produção de sialofosfoproteína dentinária (DSPP), pelo ensaio imunoenzimático ELISA. Foi observado que as concentrações de 5 e 10 µg/mL de LL-37 não foram citotóxicas e ainda aumentaram, em geral, a viabilidade celular (p<0,05), sendo que os maiores valores de absorbância foram observados no 3° dia de contato. As concentrações testadas também não induziram genotoxicidade, após 7 dias de contato, tendo sido genotóxico apenas o grupo controle positivo (EMS) (p<0,05). Ainda, não foi observado diferença estatisticamente significativa na produção de nitrito, pelas células expostas ao LL-37 após 7 dias, em ambas as concentrações. A análise do ciclo celular, evidenciou maior porcentual de células na fase G0/G1, em todos os grupos (p<0,05). Quando estes foram comparados, foi observado maior quantidade de células na fase G0/G1 na concentração de... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract : The LL 37 peptide (human derived cathelicidin) is released by some human cells and able of neutralizing the tissues that present lipopolysaccharide (LPS), as well as, attracts pulp cells and induces angiogenesis; characteristics that makes it a possible adjunct for regeneration of the dentin-pulp complex. The aim of this study was evaluate in vitro the biocompatibility of LL-37 in the concentrations of 5 and 10 µg/mL, and its possible performance in the differentiation of dental pulp stem cells (DPSC) into odontoblasts-like cells. For this purpose, it was evaluated: (a) the cytotoxicity by MTT assay; (b) the genotoxicity by the micronucleus test; (c) the production and quantification of nitric oxide; (d) the cell cycle, by flow cytometry; (e) the expression of genes associated with the mineralization by qRT-PCR; (f) the total protein content; (g) the alkaline phosphatase activity (ALP); and (h) the production of dentine sialofosfoprotein (DSPP) by indirect enzyme-linked immunosorbent assay (ELISA). It was observed that the concentrations of 5 and 10 µg/ml of LL-37 were not cytotoxic, in addition to they increased, in general, the cell viability (p<0,05). Moreover, higher absorbance values were observed on 3rd day of contact. After 7 days, the tested concentrations also did not induce genotoxicity, (p<0,05); only the positive control group (EMS) was genotoxic (p<0.05). Furthermore, there was not statistical significance in the nitrite production by the cells exposed to LL-37 for 7 days, in both concentrations. The cell cycle test showed higher percentage of cells in the phase G0/G1 in all groups (p<0.05). When they were compared, it was noticied that concentration of 10 ug/ml of LL-37 arrested the cells in G0/G1 compared to the control group (p<0.05). On the other hand, the control group, exhibited higher amount of cells in G2 and mitosis...(Resumo completo, clicar acesso eletrônico abaixo)
Doutor
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Zreika, Sami. "Etude de l'impact de la protéine antimicrobienne humaine hCAP18/LL-37 sur le cancer du sein." Thesis, Tours, 2011. http://www.theses.fr/2011TOUR4052.
Full textAbstract:
Le peptide hCAP18/LL-37, une partie de la défense immunitaire innée, a maintenant été reconnu comme multifonctionnelle pour les cellules eucaryotes. Nos études démontrent sa contribution au développement du cancer, montrant qu'il est surexprimé dans la plupart des tumeurs mammaires humaines, active la signalisation la famille de ERBB et augmente le potentiel métastatique des cellules cancéreuses du sein. Notre comparaison des deux lignées du cancer du sein n'a pas révélé de récepteurs communs, mais une structure peptidique identiques mais de chiralité différente est pré requis pour le peptide dans toutes ses activités. Nous émettons l'hypothèse que LL-37 active indirectement des récepteurs transmembranaires en se liant à la membrane cellulaire. Des peptides tronqués dérivés de LL-37 inhibent ses activités et peuvent aider à concevoir une future thérapie anticancéreuseThe peptide hCAP18/LL-37, part of the innate immune defense, has now been recognized as multifunctional for eukaryotic cells. Our studies demonstrate its contribution to cancer development, showing that it is overexpressed in most human breast tumors, activates ERBB signaling and increases the metastatic potential of breast cancer cells. Our comparison on two breast cancer lines did not reveal any common receptors but identical structural prerequisites for the peptide in all its activities. We hypothesize that LL-37 indirectly activates transmembrane receptors by attaching to the cellular membrane. Truncated derivatives inhibit its activities and may help to design a future anticancer therapy
Book chapters on the topic "Peptide LL-37"
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Beaumont, Paula E., Hsin-Ni Li, and Donald J. Davidson. "LL-37: An Immunomodulatory Antimicrobial Host Defence Peptide." In Antimicrobial Peptides and Innate Immunity, 97–121. Basel: Springer Basel, 2012. http://dx.doi.org/10.1007/978-3-0348-0541-4_4.
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Nylén, Frank, Peter Bergman, Gudmundur H. Gudmundsson, and Birgitta Agerberth. "Assays for Identifying Inducers of the Antimicrobial Peptide LL-37." In Methods in Molecular Biology, 271–81. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6737-7_19.
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Wang, Guangshun, Jayaram Lakshmaiah Narayana, Biswajit Mishra, Yingxia Zhang, Fangyu Wang, Chunfeng Wang, D. Zarena, Tamara Lushnikova, and Xiuqing Wang. "Design of Antimicrobial Peptides: Progress Made with Human Cathelicidin LL-37." In Advances in Experimental Medicine and Biology, 215–40. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-3588-4_12.
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Sorkin, M., F. Jacobsen, D. Mittler, T. Hirsch, A. Gerhards, M. Lehnhardt, H. U. Steinau, and L. Steinstraesser. "Kutane adenovirale Gentherapie mit humanem Host Defense Peptid LL-37 in infizierten Verbrennungswunden der Ratte." In Chirurgisches Forum 2006, 357–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-34668-6_123.
Full textConference papers on the topic "Peptide LL-37"
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Biondi, Barbara, Silvia Millan, Fernando Formaggio, Alessandra Semenzato, and Cristina Peggion. "Synthesis and conformationof short peptides modeled after peptide LL-37." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.195.
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Lee, Jia-Yi, Chung-Yih Wang, Chi-Fang Huang, and An-Ting Cheng. "Interdigitated electrodes based on impedance biosensor for sensing peptide LL-37." In 2011 33rd Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2011. http://dx.doi.org/10.1109/iembs.2011.6089899.
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Wang, Guangshun. "Design potent peptide antibiotics against the ESKAPE pathogens based on human antimicrobial peptide LL-37." In 4th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2018. http://dx.doi.org/10.3390/ecmc-4-05882.
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Lu, Xiuxiu, Qi Zhang, Guowei Song, Xiaodai Cui, Jian Yang, and Baoyuan Zhang. "The Changes of Plasma Antibacterial Peptide ll-37 in the Bloodstream Infected Children." In Selection of Abstracts From NCE 2016. American Academy of Pediatrics, 2018. http://dx.doi.org/10.1542/peds.141.1_meetingabstract.331.
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McCaskill, Michael L., Jill A. Poole, Diane S. Allen-Gipson, Jane M. DeVasure, and Todd A. Wyatt. "Ethanol Consumption Leads To Reduced Levels Of Lung Tissue Vitamin D And Anti-Microbial Peptide LL-37 In C57Bl/6 Mice." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4670.
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Krasnodembskaya, Anna, Yuanlin Song, Jae-Woo Lee, and Michael A. Matthay. "Human Mesenchymal Stem Cells Exert Antimicrobial Activity In Vitro And In Vivo In Part Through The Secretion Of The Antimicrobial Peptide LL-37." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1246.
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Schrumpf, Jasmijn, Renate Verhoosel, and Pieter Hiemstra. "Vitamin D-mediated expression of the antimicrobial peptide hCAP18/LL-37 and killing of non-typeablehaemophilus influenzae(NTHi) is reduced after 14 days exposure to TNF-α and IL-1β in primary bronchial epithelial cells (PBEC)." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.oa1785.
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Valencia, Yeny Y. P., Gabriel C. A. da Hora, and Thereza A. Soares. "INTERAÇÃO DE AGREGADOS DE POPG NA PRESENÇA DE PEPTIDEO ANTIMICROBIANOS LL 37." In Encontro Anual da biofisica 2019. São Paulo: Editora Blucher, 2019. http://dx.doi.org/10.5151/biofisica2019-23.
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