Letteratura scientifica selezionata sul tema "LL-37 peptid"
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Articoli di riviste sul tema "LL-37 peptid"
Guo, Fang-Fang, e Jing-Yuan Fang. "Antimicrobial peptide LL-37 and gastrointestinal diseases". World Chinese Journal of Digestology 22, n. 35 (2014): 5454. http://dx.doi.org/10.11569/wcjd.v22.i35.5454.
Testo completoBucki, Robert, Katarzyna Leszczyńska, Andrzej Namiot e Wojciech Sokołowski. "Cathelicidin LL-37: A Multitask Antimicrobial Peptide". Archivum Immunologiae et Therapiae Experimentalis 58, n. 1 (5 gennaio 2010): 15–25. http://dx.doi.org/10.1007/s00005-009-0057-2.
Testo completoRapala-Kozik, Maria, Oliwia Bochenska, Marcin Zawrotniak, Natalia Wolak, Grzegorz Trebacz, Mariusz Gogol, Dominika Ostrowska, Wataru Aoki, Mitsuyoshi Ueda e Andrzej Kozik. "Inactivation of the Antifungal and Immunomodulatory Properties of Human Cathelicidin LL-37 by Aspartic Proteases Produced by the Pathogenic Yeast Candida albicans". Infection and Immunity 83, n. 6 (6 aprile 2015): 2518–30. http://dx.doi.org/10.1128/iai.00023-15.
Testo completoSieprawska-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, n. 12 (dicembre 2004): 4673–79. http://dx.doi.org/10.1128/aac.48.12.4673-4679.2004.
Testo completoMartynowycz, Michael, Amy Rice, Konstantin Andreev, Thatyane M. Nobre Pavinatto, Jeff Wereszczynski e David Gidalevitz. "Interaction of Antimicrobial Peptide Ll-37 with Lipopolysaccharides". Biophysical Journal 116, n. 3 (febbraio 2019): 45a. http://dx.doi.org/10.1016/j.bpj.2018.11.285.
Testo completoYusuf, Muhammad, Wanda Destiarani, Ade Rizqi Ridwan Firdaus, Fauzian Giansyah Rohmatulloh, Mia Tria Novianti, Gita Widya Pradini e Reiva Farah Dwiyana. "Residual Interactions of LL-37 with POPC and POPE:POPG Bilayer Model Studied by All-Atom Molecular Dynamics Simulation". International Journal of Molecular Sciences 23, n. 21 (2 novembre 2022): 13413. http://dx.doi.org/10.3390/ijms232113413.
Testo completoZhao, Chengquan, Tung Nguyen, Lee Ming Boo, Teresa Hong, Cesar Espiritu, Dmitri Orlov, Wei Wang, Alan Waring e Robert I. Lehrer. "RL-37, an Alpha-Helical Antimicrobial Peptide of the Rhesus Monkey". Antimicrobial Agents and Chemotherapy 45, n. 10 (1 ottobre 2001): 2695–702. http://dx.doi.org/10.1128/aac.45.10.2695-2702.2001.
Testo completoBals, Robert, Xiaorong Wang, Michael Zasloff e James M. Wilson. "The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface". Proceedings of the National Academy of Sciences 95, n. 16 (4 agosto 1998): 9541–46. http://dx.doi.org/10.1073/pnas.95.16.9541.
Testo completoIshvaanjil, Bayartbat, Yu-Jin Jung, Uyangaa Temuujin, Soon-Youl Lee e Kwon-Kyoo Kang. "HETEROLOGOUS EXPRESSION OF ANTIMICROBIAL PEPTIDE LL-37 IN CHINESE CABBAGE WITH ENHANCED RESISTANCE TO PATHOGENS". Mongolian Journal of Agricultural Sciences 13, n. 2 (22 giugno 2015): 124–30. http://dx.doi.org/10.5564/mjas.v13i2.531.
Testo completoRidyard, Kylen E., e Joerg Overhage. "The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent". Antibiotics 10, n. 6 (29 maggio 2021): 650. http://dx.doi.org/10.3390/antibiotics10060650.
Testo completoTesi sul tema "LL-37 peptid"
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/.
Testo completoAufgrund 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.
Habes, Chahrazed. "Stimulation du signal calcique et de la migration des cellules cancéreuses mammaires par le peptide LL-37 : un mécanisme d’attachement membranaire impliquant les glycosaminoglycanes et les syndécanes". Thesis, Tours, 2019. http://www.theses.fr/2019TOUR3807.
Testo completoInitially characterized by its antimicrobial activities, LL-37 has also been shown to significantly contribute to tumor development. On breast cancer cell lines, LL-37 increases intracellular calcium and their migration via the activation of PI3K/AKT signaling. Its all-D enantiomer (D)-LL-37 induces similar effects, which excludes an protein-protein interaction of LL-37 in a classic ligand-receptor manner. Its structure of an amphipathic a-helix with a net charge of +6 gave rise to the hypothesis that the peptide uses the negative charges of sulfoglycans or sialic acids to facilitate its attachment to the cell membrane and to induce its activities. Whereas several lectins, specifically attaching to sialylated or sulfated structures, blocked the activities of LL-37 on both calcium increase and cell migration, the suppression of several sialyltransferases had no effect. However, the competitive use of glycoaminoglycans (GAG) and chrondroitin and sulfated heparin, or treatment of the cell surface with chondroitinase and heparinase resulted in an activity loss of 50-100%. Similar results were obtained by confirmed by blocking the synthesis of GAGs with Methylumbelliferyl β-D-xyloside, and by suppression of glycan sulfurylation by sodium chlorate. Using a candidate approach by suppressing proteoglycan synthesis by RNA interference, syndecan 4 was shown to be involved in the activities of LL-37. This leads to the conclusion that sulfated GAGs linked to syndecans 4 guides the association of LL-37 to the membrane of cancer cells, thus being a mediator of its activities
El, Abbouni Sarah. "Microencapsulation of LL-37 Antimicrobial Peptide in PLGA". Digital WPI, 2016. https://digitalcommons.wpi.edu/etd-theses/235.
Testo completoFilewod, Niall Christopher Jack. "Immunomodulatory effects of LL-37 in the epithelia". Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/927.
Testo completoCarlsson, Martin, e Johan Humlén. "Effekter av den antimikrobiella peptiden LL-37 på humana osteoblasters viabilitet". Thesis, Malmö högskola, Odontologiska fakulteten (OD), 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:mau:diva-19902.
Testo completoGhannad, Mona. "Design and Synthesis of Collagen-binding Anti-microbial Proteins". Thèse, Université d'Ottawa / University of Ottawa, 2011. http://hdl.handle.net/10393/19981.
Testo completoLi, 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.
Testo completoScience, Faculty of
Microbiology and Immunology, Department of
Graduate
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/.
Testo completoMilhan, 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.
Testo completoBanca: 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
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.
Testo completoThe 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
Capitoli di libri sul tema "LL-37 peptid"
Sorkin, M., F. Jacobsen, D. Mittler, T. Hirsch, A. Gerhards, M. Lehnhardt, H. U. Steinau e 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.
Testo completoBeaumont, Paula E., Hsin-Ni Li e 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.
Testo completoNylén, Frank, Peter Bergman, Gudmundur H. Gudmundsson e 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.
Testo completoWang, Guangshun, Jayaram Lakshmaiah Narayana, Biswajit Mishra, Yingxia Zhang, Fangyu Wang, Chunfeng Wang, D. Zarena, Tamara Lushnikova e 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.
Testo completoAtti di convegni sul tema "LL-37 peptid"
Biondi, Barbara, Silvia Millan, Fernando Formaggio, Alessandra Semenzato e 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.
Testo completoLee, Jia-Yi, Chung-Yih Wang, Chi-Fang Huang e 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.
Testo completoWang, 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.
Testo completoLu, Xiuxiu, Qi Zhang, Guowei Song, Xiaodai Cui, Jian Yang e 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.
Testo completoValencia, Yeny Y. P., Gabriel C. A. da Hora e 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.
Testo completoMcCaskill, Michael L., Jill A. Poole, Diane S. Allen-Gipson, Jane M. DeVasure e 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.
Testo completoKrasnodembskaya, Anna, Yuanlin Song, Jae-Woo Lee e 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.
Testo completoSchrumpf, Jasmijn, Renate Verhoosel e 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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