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    • Proszę używać tego identyfikatora do cytowań lub wstaw link do tej pozycji: http://hdl.handle.net/11320/16595
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    Pole DCWartośćJęzyk
    dc.contributor.authorPiktel, Ewelina-
    dc.contributor.authorWnorowska, Urszula-
    dc.contributor.authorCieśluk, Mateusz-
    dc.contributor.authorDeptuła, Piotr-
    dc.contributor.authorPogoda, Katarzyna-
    dc.contributor.authorMisztalewska-Turkowicz, Iwona-
    dc.contributor.authorPaprocka, Paulina-
    dc.contributor.authorNiemirowicz-Laskowska, Katarzyna-
    dc.contributor.authorWilczewska, Agnieszka Z.-
    dc.contributor.authorJanmey, Paul A.-
    dc.contributor.authorBucki, Robert-
    dc.date.accessioned2024-06-03T07:57:49Z-
    dc.date.available2024-06-03T07:57:49Z-
    dc.date.issued2019-
    dc.identifier.citationJournal of Nanobiotechnology, Vol. 17 (2019), Article number: 22pl
    dc.identifier.issn1477-3155-
    dc.identifier.urihttp://hdl.handle.net/11320/16595-
    dc.description.abstractBackground: Human plasma gelsolin (pGSN) is a multifunctional actin-binding protein involved in a variety of biological processes, including neutralization of pro-infammatory molecules such as lipopolysaccharide (LPS) and lipoteichoic acid (LTA) and modulation of host infammatory response. It was found that PBP10, a synthetic rhodamine B-conjugated peptide, based on the phosphoinositide-binding site of pGSN, exerts bactericidal activity against Grampositive and Gram-negative bacteria, interacts specifcally with LPS and LTA, and limits microbial-induced infammatory efects. The therapeutic efciency of PBP10 when immobilized on the surface of iron oxide-based magnetic nanoparticles was not evaluated, to date. Results: Using the human keratinocyte cell line HaCaT stimulated by bacterially-derived LPS and LTA as an in vitro model of bacterial infection, we examined the anti-infammatory efects of nanosystems consisting of iron oxidebased magnetic nanoparticles with aminosilane (MNP@NH2) or gold shells (MNP@Au) functionalized by a set of peptides, derived from the phosphatidylinositol 4,5-bisphosphate (PIP2)-binding site of the human plasma protein gelsolin, which also binds LPS and LTA. Our results indicate that these nanosystems can kill both Gram-positive and Gram-negative bacteria and limit the production of infammatory mediators, including nitric oxide (NO), reactive oxygen species (ROS), and interleukin-8 (IL-8) in the response to heat-killed microbes or extracted bacterial cell wall components. The nanoparticles possess the potential to improve therapeutic efcacy and are characterized by lower toxicity and improved hemocompatibility when compared to free peptides. Atomic force microscopy (AFM) showed that these PBP10-based nanosystems prevented changes in nanomechanical properties of cells that were otherwise stimulated by LPS. Conclusions: Neutralization of endotoxemia-mediated cellular efects by gelsolin-derived peptides and PBP10-containing nanosystems might be considered as potent therapeutic agents in the improved therapy of bacterial infections and microbial-induced infammation.pl
    dc.description.sponsorshipThis work was fnancially supported by the National Science Center, Poland under Grant: UMO-2015/17/B/NZ6/03473 (to RB) and Medical University of Bialystok (N/ST/ZB/18/002/1162 and N/ST/ZB/18/001/1162 (to RB) and N/ST/MN/18/002/1162 (to EP). Part of the study was conducted with the use of equipment purchased by the Medical University of Białystok as part of the RPOWP 2007-2013 funding, Priority I, Axis 1.1, contract No. UDARPPD.01.01.00-20-001/15-00 dated 26.06.2015. The physicochemical studies were performed in Centre of Synthesis and Analysis BioNanoTechno of the University of Bialystok (POPW.01.03.00-20-034/09-00 and POPW.01.03.00-20004/11 projects). EP acknowledges a doctoral scholarship from Polpharma Scientifc Foundation, Poland. PAJ and RB acknowledge support from NIH grant GM111942-01.pl
    dc.language.isoenpl
    dc.publisherBioMed Central (BMC)pl
    dc.rightsUznanie autorstwa 4.0 Międzynarodowe*
    dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
    dc.subjectGelsolinpl
    dc.subjectInfammationpl
    dc.subjectSkin diseasespl
    dc.subjectPBP10pl
    dc.subjectMagnetic nanoparticlespl
    dc.titleInhibition of inflammatory response in human keratinocytes by magnetic nanoparticles functionalized with PBP10 peptide derived from the PIP2-binding site of human plasma gelsolinpl
    dc.typeArticlepl
    dc.rights.holder© The Author(s) 2019. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/)pl
    dc.identifier.doi10.1186/s12951-019-0455-5-
    dc.description.EmailRobert Bucki: buckirobert@gmail.compl
    dc.description.AffiliationEwelina Piktel - Department of Microbiological and Nanobiomedical Engineering, Medical University of Bialystokpl
    dc.description.AffiliationUrszula Wnorowska - Department of Microbiological and Nanobiomedical Engineering, Medical University of Bialystokpl
    dc.description.AffiliationMateusz Cieśluk - Department of Microbiological and Nanobiomedical Engineering, Medical University of Bialystokpl
    dc.description.AffiliationPiotr Deptula - Department of Microbiological and Nanobiomedical Engineering, Medical University of Bialystokpl
    dc.description.AffiliationKatarzyna Pogoda - IInstitute of Nuclear Physics Polish Academy of Sciencespl
    dc.description.AffiliationIwona Misztalewska‑Turkowicz - Institute of Chemistry, University of Białystokpl
    dc.description.AffiliationPaulina Paprocka - Department of Microbiology and Immunology, The Faculty of Medicine and Health Sciences of the Jan Kochanowski University in Kielcepl
    dc.description.AffiliationKatarzyna Niemirowicz‑Laskowska - Department of Microbiological and Nanobiomedical Engineering, Medical University of Bialystokpl
    dc.description.AffiliationAgnieszka Z. Wilczewska - Institute of Chemistry, University of Białystokpl
    dc.description.AffiliationPaul A. Janmey - Department of Physiology and Institute for Medicine and Engineering, University of Pennsylvaniapl
    dc.description.AffiliationRobert Bucki - Department of Microbiological and Nanobiomedical Engineering, Medical University of Bialystokpl
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    dc.description.volume17pl
    dc.identifier.citation2Journal of Nanobiotechnologypl
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