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Steckiewicz KP, Cieciórski P, Barcińska E, et al. Int J Nanomedicine. 2022;17:495–517. Our authors have advised that the funding source number listed in the Acknowledgment section on page 513 was incorrect. The sentence should read from “This work was supported by PRELUDIUM grant 2017/27/N/NZ7/0267 from the Polish National Science Centre…” to “This work was supported by PRELUDIUM grant 2017/27/N/NZ7/02675 from the Polish National Science Centre…” The authors apologize for this oversight.

Karol P Steckiewicz,1 Piotr Cieciórski,2 Ewelina Barcińska,1 Maciej Jaśkiewicz,3 Magdalena Narajczyk,4 Marta Bauer,3 Wojciech Kamysz,3 Elżbieta Megiel,2 Iwona Inkielewicz-Stepniak1 1Department of Pharmaceutical Pathophysiology, Faculty of Pharmacy, Medical University of Gdansk, Gdansk, Poland; 2Faculty of Chemistry, University of Warsaw, Warsaw, Poland; 3Department of Inorganic Chemistry, Faculty of Pharmacy, Medical University of Gdansk, Gdansk, Poland; 4Laboratory of Electron Microscopy, Faculty of Biology, University of Gdansk, Gdansk, PolandCorrespondence: Iwona Inkielewicz-Stepniak Tel +48 58 349 1516Fax +48 58 349 1517Email iinkiel@gumed.edu.plPurpose: Periodontal disease (PD), defined as oral inflammation caused by dental plaque, is an emerging problem. PD may lead to tooth loss, and treatment options are limited. In this study, we designed, synthesized, and characterized silver nanoparticles (AgNPs) conjugated with chlorhexidine (AgNPs-CHL) or metronidazole (AgNPs-PEG-MET) to determine whether they can be used to treat PDs.Materials and Methods: AgNPs were synthesized and characterized by transmission electron microscopy, UV-vis spectrometry, thermogravimetric analyses, and dynamic light scattering. We determined the safety and the antimicrobial and anti-inflammatory properties of synthesized AgNPs in an in vitro model of periodontitis. Antimicrobial properties were determined by measuring the minimum inhibitory concentration (MIC) and minimum biofilm eradication concentration (MBEC) on reference strains of bacteria and fungi. Human gingival fibroblast (HGF-1), murine macrophage (RAW264.7) and human foetal osteoblast (hFOB1.19) cells were used in the study. Lipopolysaccharide (LPS) was used to induce inflammation. Cytokine levels were measured using an enzyme-linked immunosorbent assay; metalloproteinase expression was measured using Western blotting.Results: The synthesized AgNPs were spherical and narrow-dispersed with an av

Karol P Steckiewicz,1 Piotr Cieciórski,2 Ewelina Barcińska,1 Maciej Jaśkiewicz,3 Magdalena Narajczyk,4 Marta Bauer,3 Wojciech Kamysz,3 Elżbieta Megiel,2 Iwona Inkielewicz-Stepniak1 1Department of Pharmaceutical Pathophysiology, Faculty of Pharmacy, Medical University of Gdansk, Gdansk, Poland; 2Faculty of Chemistry, University of Warsaw, Warsaw, Poland; 3Department of Inorganic Chemistry, Faculty of Pharmacy, Medical University of Gdansk, Gdansk, Poland; 4Laboratory of Electron Microscopy, Faculty of Biology, University of Gdansk, Gdansk, PolandCorrespondence: Iwona Inkielewicz-Stepniak Tel +48 58 349 1516Fax +48 58 349 1517Email iinkiel@gumed.edu.plPurpose: Periodontal disease (PD), defined as oral inflammation caused by dental plaque, is an emerging problem. PD may lead to tooth loss, and treatment options are limited. In this study, we designed, synthesized, and characterized silver nanoparticles (AgNPs) conjugated with chlorhexidine (AgNPs-CHL) or metronidazole (AgNPs-PEG-MET) to determine whether they can be used to treat PDs.Materials and Methods: AgNPs were synthesized and characterized by transmission electron microscopy, UV-vis spectrometry, thermogravimetric analyses, and dynamic light scattering. We determined the safety and the antimicrobial and anti-inflammatory properties of synthesized AgNPs in an in vitro model of periodontitis. Antimicrobial properties were determined by measuring the minimum inhibitory concentration (MIC) and minimum biofilm eradication concentration (MBEC) on reference strains of bacteria and fungi. Human gingival fibroblast (HGF-1), murine macrophage (RAW264.7) and human foetal osteoblast (hFOB1.19) cells were used in the study. Lipopolysaccharide (LPS) was used to induce inflammation. Cytokine levels were measured using an enzyme-linked immunosorbent assay; metalloproteinase expression was measured using Western blotting.Results: The synthesized AgNPs were spherical and narrow-dispersed with an av

Background: Candida albicans yeast produces 10 distinct secreted aspartic proteases (Saps), which are some of the most important virulence factors of this pathogenic fungus. One of the suggested roles of Saps is their deregulating effect on various proteolytic cascades that constitute the major homeostatic systems in human hosts, including blood coagulation, fibrinolysis, and kallikrein-kinin systems. This study compared the characteristics of the action of all 10 Saps on human kininogens, which results in generating proinflammatory bradykinin-related peptides (kinins). Results: Recombinant forms of Saps, heterologously overexpressed in Pichia pastoris were applied. Except for Sap7 and Sap10, all Saps effectively cleaved the kininogens, with the highest hydrolytic activity toward the low-molecular-mass form (LK). Sap1-6 and 8 produced a biologically active kinin - Met-Lys-bradykinin - and Sap3 was exceptional in terms of the kinin-releasing yield (>60% LK at pH 5.0 after 24 hours). Des-Arg1-bradykinin was released from LK by Sap9 at a comparably high yield, but this peptide was assumed to be biologically inactive because it was unable to interact with cellular B2-type kinin receptors. However, the collaborative actions of Sap9 and Sap1, -2, -4-6, and -8 on LK rerouted kininogen cleavage toward the high-yield release of the biologically active Met-Lys-bradykinin. Conclusions: Our present results, together with the available data on the expression of individual SAP genes in candidal infection models, suggest a biological potential of Saps to produce kinins at the infection foci. The kinin release during candidiasis can involve predominant and complementary contributions of two different Sap3- and Sap9-dependent mechanisms.

Zinc binding to P113 (or demegen), a 12 amino acid (AKRHHGYKRKFH-NH2) fragment of histatin 5, was investigated by means of NMR and CD techniques, yielding delineation of the metal binding site and the 3D structure of the complex in water and in DMSO as well. The three His imidazole and the N-terminus nitrogens were found to act as the zinc coordinating atoms. A comparison with the previously reported Cu(II)-P113 complex disclosed that the two structures were rather diverse, in spite of an identical donor set. The two complexes were also tested for their antimicrobial activity in vitro against seven bacteria and two yeast strains: a minor activity of both complexes vs that of free ligand was given evidence, suggesting both metal ions may possibly play a negative role in vivo.