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Strömstedt, Adam A., DocentORCID iD iconorcid.org/0000-0001-9070-6944
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Ismail, N. O., Odendaal, C., Serem, J. C., Strömstedt, A. A., Bester, M. J., Sayed, Y., . . . Gaspar, A. R. (2019). Antimicrobial function of short amidated peptide fragments from the tick-derived OsDef2 defensin.. Journal of Peptide Science, 25(12), Article ID e3223.
Öppna denna publikation i ny flik eller fönster >>Antimicrobial function of short amidated peptide fragments from the tick-derived OsDef2 defensin.
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2019 (Engelska)Ingår i: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 25, nr 12, artikel-id e3223Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Previously Os, a 22 amino acid sequence of a defensin from the soft tick Ornithodoros savignyi, was found to kill Gram-positive and Gram-negative bacteria at low micromolar concentrations. In this study, we evaluated synthetic peptide analogues of Os for antibacterial activity with an aim to identify minimalized active peptide sequences and in so doing obtain a better understanding of the structural requirements for activity. Out of eight partially overlapping sequences of 10 to 12 residues, only Os(3-12) and Os(11-22) exhibit activity when screened against Gram-positive and Gram-negative bacteria. Carboxyamidation of both peptides increased membrane-mediated activity, although carboxyamidation of Os(11-22) negatively impacted on activity against Staphylococcus aureus. The amidated peptides, Os(3-12)NH2 and Os(11-22)NH2 , have minimum bactericidal concentrations of 3.3 μM against Escherichia coli. Killing was reached within 10 minutes for Os(3-12)NH2 and only during the second hour for Os(11-22)NH2 . In an E. coli membrane liposome system, both Os and Os(3-12)NH2 were identified as membrane disrupting while Os(11-22)NH2 was less active, indicating that in addition to membrane permeabilization, other targets may be involved in bacterial killing. In contrast to Os, the membrane disruptive effect of Os(3-12)NH2 did not diminish in the presence of salt. Neither Os nor its amidated derivatives caused human erythrocyte haemolysis. The contrasting killing kinetics and effects of amidation together with structural and liposome leakage data suggest that the 3-12 fragment relies on a membrane disruptive mechanism while the 11-22 fragment involves additional target mechanisms. The salt-resistant potency of Os(3-12)NH2 identifies it as a promising candidate for further development.

Nyckelord
antimicrobial resistance, carboxyamidation, mechanism of action, membrane permeabilization, minimalized peptide, tick defensin
Nationell ämneskategori
Läkemedelskemi
Identifikatorer
urn:nbn:se:uu:diva-401412 (URN)10.1002/psc.3223 (DOI)31713951 (PubMedID)
Tillgänglig från: 2020-01-07 Skapad: 2020-01-07 Senast uppdaterad: 2020-02-05Bibliografiskt granskad
Malekkhaiat Häffner, S., Nyström, L., Strömstedt, A. A., Li, L., van der Plas, M. J. & Malmsten, M. (2019). Nanoclay-induced bacterial flocculation for infection confinement. Journal of Colloid and Interface Science, 562, 71-80
Öppna denna publikation i ny flik eller fönster >>Nanoclay-induced bacterial flocculation for infection confinement
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2019 (Engelska)Ingår i: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 562, s. 71-80Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Effects of size and charge of anionic nanoclays on their interactions with bacteria-mimicking lipid membranes, bacterial lipopolysaccharide (LPS), and Gram-negative bacteria were investigated using ellipsometry, dynamic light scattering, ζ-potential measurements, and confocal microscopy combined with Live/Dead staining. Based on particle size and charge density, three different anionic hectorite nanoclays were employed, and investigated in the presence and absence of the net cationic human antimicrobial peptide LL-37 (LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES). In the absence of this peptide, the nanoclays were found not to bind to similarly anionic bacteria-mimicking model phospholipid membranes, nor to destabilize these. Similarly, while all nanoclays induced aggregation of Escherichia coli bacteria, the flocculated bacteria remained alive after aggregation. In contrast, LL-37 alone, i.e. in the absence of nanoclay particles, displays antimicrobial properties through membrane lysis, but does not cause bacterial aggregation in the concentration range investigated. After loading the nanoclays with LL-37, potent bacterial aggregation combined with bacterial membrane lysis was observed for all nanoclay sizes and charge densities. Demonstrating the potential of these combined systems for confinement of infection, LPS-induced NF-κB activation in human monocytes was found to be strongly suppressed after nanoclay-mediated aggregation, with a wide tolerance for nanoparticle size and charge density.

Ort, förlag, år, upplaga, sidor
Elsevier, 2019
Nyckelord
Antimicrobial, Bacteria flocculation, Infection confinement, Membrane
Nationell ämneskategori
Farmaceutiska vetenskaper Läkemedelskemi
Identifikatorer
urn:nbn:se:uu:diva-401401 (URN)10.1016/j.jcis.2019.11.110 (DOI)000508752700008 ()31837621 (PubMedID)
Forskningsfinansiär
Vetenskapsrådet, 2016-05157
Tillgänglig från: 2020-01-07 Skapad: 2020-01-07 Senast uppdaterad: 2020-03-20Bibliografiskt granskad
Mohotti, S., Rajendran, S., Muhammad, T., Strömstedt, A. A., Adhikari, A., Burman, R., . . . Gunasekera, S. (2019). Screening for bioactive secondary metabolites in Sri Lankan medicinal plants by microfractionation and targeted isolation of antimicrobial flavonoids from Derris scandens. Journal of Ethnopharmacology, 246, Article ID 112158.
Öppna denna publikation i ny flik eller fönster >>Screening for bioactive secondary metabolites in Sri Lankan medicinal plants by microfractionation and targeted isolation of antimicrobial flavonoids from Derris scandens
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2019 (Engelska)Ingår i: Journal of Ethnopharmacology, ISSN 0378-8741, E-ISSN 1872-7573, Vol. 246, artikel-id 112158Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Ethnopharmacological relevance: Sri Lanka is known to have very diverse flora. Many of these species are used for plant-based remedies, which form the integral part of two Sri Lankan systems of traditional medicine, Ayurveda and Deshiya Chikitsa. Despite their widespread use, only a limited number of studies have probed into the scientific evidence for bioactivity of these medicinal plants. Such studies rarely progress to the identification of bioactive natural products. Aim of the study: The primary aim was to develop a bioactivity screening method and apply it to 50 Sri Lankan medicinal plants where antimicrobial properties could be relevant for its traditional use. The subsequent aim was the progression into defining and characterising potent isolates within targeted compound classes from such plants, i.e. Derris scandens and its antimicrobial flavonoids. Material and methods: The plant collection comprised 24 species of Fabaceae, 15 Rubiaceae, 7 Solanaceae and 4 Cucurbitaceae plants. These 50 species were collected based on their ethnopharmacological importance and use in Sri Lankan traditional medicine. Crude extracts from each species were initially subjected to radial disc diffusion and microdilution assays. Subsequently, aqueous extracts of all plants were microfractionated in deep well plates using reversed-phase HPLC. Fractions were tested for antibacterial and cytotoxic activities and masses of target bioactive compounds were identified using mass spectrometry. Bioactive compounds with the masses identified through microfractions were isolated from Derris scandens using reversed-phase HPLC. The isolated pure compounds were characterised using LC-MS and NMR. Results: Crude aqueous extracts from 19 species showed activity against Gram-positive bacteria (Staphylococcus aureus and Bacillus cereus) in the radial disc diffusion assay. Crude aqueous extracts from 34 plant species and organic extracts from 46 plant species were active against S. aureus (<= 4 mg mL(-1)) in the microdilution assay. Microfractionation demonstrated antibacterial activity for 19 plants and cytotoxicity for 6 plants. Furthermore, target bioactive compounds and their molecular ions were identified during microfractionation. Dalpanitin and vicenin-3, two of the flavonoids isolated from Derris scandens gave MICs of 23 mu g mL(-1) against S. aureus. Dalpanitin also exhibited relevant MICs on Gram-negative bacteria (94 mu g mL(-1)) against Escherichia coli and Pseudomonas aeruginosa). Conclusion: The microfractionation protocol developed in this study enabled time-efficient screening of many plants species, using a small quantity of sample material. In addition, microfractionation served as a guiding tool for identifying individual antimicrobial compounds. Through this process, flavonoids were isolated from Derris scandens, out of which dalpanitin and vicenin-3 showed activity in the low micromolar range. The high hit rate for in vitro antibacterial properties from this ethnopharmacologically guided sample collection gives credence to Sri Lankan traditional herbal medicine as a source for drug discovery.

Nyckelord
Sri Lanka, Medicinal plants, Microfractionation, Antimicrobial activity, Cytotoxicity, Flavonoids
Nationell ämneskategori
Farmakologi och toxikologi
Identifikatorer
urn:nbn:se:uu:diva-397136 (URN)10.1016/j.jep.2019.112158 (DOI)000493211800010 ()31421182 (PubMedID)
Forskningsfinansiär
Vetenskapsrådet, 2013-06672
Tillgänglig från: 2019-11-28 Skapad: 2019-11-28 Senast uppdaterad: 2019-11-28Bibliografiskt granskad
Forde, E., Shafiy, G., Fitzgerald-Hughes, D., Strömstedt, A. A. & Devocelle, M. (2018). Action of antimicrobial peptides and their prodrugs on model and biological membranes. Paper presented at 7th International Meeting on Antimicrobial Peptides, AUG 25-27, 2017, Univ Copenhagen, Copenhagen, DENMARK. Journal of Peptide Science, 24(7), Article ID e3086.
Öppna denna publikation i ny flik eller fönster >>Action of antimicrobial peptides and their prodrugs on model and biological membranes
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2018 (Engelska)Ingår i: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 24, nr 7, artikel-id e3086Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Antimicrobial peptides (AMPs) are promising broad-spectrum antibiotic candidates in the wake of multi-drug resistant pathogens. Their clinical use still requires a solution based on lead optimisation and/ or formulation to overcome certain limitations, such as unwanted cytotoxicity. A prodrug approach could overcome this safety barrier and can be achieved through reversible reduction or neutralisation of the AMPs' net cationic charge. By prodrug activation through pathogen associated enzymes, this approach could increase the therapeutic index of membrane active peptides. P18, a cecropin/ magainin hybrid, and WMR, a myxinidin analogue from hagfish, were used as templates for the design strategy. The membrane permeabilizing activities of these AMPs and their prodrugs are reported here for liposomes of either Escherichia coli polar lipid extract or a human model lipid system of phosphatidylcholine and cholesterol. These results are compared with their antibacterial and haemolytic activities. Overall, correlation between liposome permeabilization and the corresponding bioactivity is observed and indicate that the broad-spectrum antibacterial effect exerted by these peptides is associated with membrane disruption. Furthermore, the prodrug modification had a general negative influence on membrane disruption and bioactivity, notably as much on bacterial as on human membranes. This prodrug strategy is particularly successful when complete neutralisation of the AMP's net charge occurs. Thus, on-target selectivity between bacterial and human membranes can be improved, which may be used to prevent the unnecessary exposure of host cells and commensal bacteria to active AMPs.

Ort, förlag, år, upplaga, sidor
WILEY, 2018
Nyckelord
antimicrobial peptides, liposomes, membrane permeabilization, prodrugs, therapeutic index
Nationell ämneskategori
Farmaceutiska vetenskaper
Identifikatorer
urn:nbn:se:uu:diva-362847 (URN)10.1002/psc.3086 (DOI)000440144700002 ()29799150 (PubMedID)
Konferens
7th International Meeting on Antimicrobial Peptides, AUG 25-27, 2017, Univ Copenhagen, Copenhagen, DENMARK
Tillgänglig från: 2018-10-15 Skapad: 2018-10-15 Senast uppdaterad: 2018-10-15Bibliografiskt granskad
Gunasekera, S., Muhammad, T., Strömstedt, A. A., Rosengren, K. J. & Göransson, U. (2018). Alanine and Lysine Scans of the LL-37-Derived Peptide Fragment KR-12 Reveal Key Residues for Antimicrobial Activity. ChemBioChem (Print), 19(9), 931-939
Öppna denna publikation i ny flik eller fönster >>Alanine and Lysine Scans of the LL-37-Derived Peptide Fragment KR-12 Reveal Key Residues for Antimicrobial Activity
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2018 (Engelska)Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 19, nr 9, s. 931-939Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The human host defence peptide LL-37 is a broad-spectrum antibiotic with immunomodulatory functions. Residues 18-29 in LL-37 have previously been identified as a minimal peptide (KR-12) that retains antibacterial activity with decreased cytotoxicity. In this study, analogues of KR-12 were generated by Ala and Lys scans to identify key elements for activity. These were tested against a panel of human pathogens and for membrane permeabilisation on liposomes. Replacements of hydrophobic and cationic residues with Ala were detrimental for antibiotic potency. Substitutions by Lys increased activity, as long as the increase in cationic density did not disrupt the amphiphilic disposition of the helical structure. Importantly, substitutions showed differential effects against different organisms. Replacement of Gln5 with Lys and Asp9 with Ala or Lys improved the broad-spectrum activity most, each resulting in up to an eightfold increase in potency against Staphylococcus aureus, Pseudomonas aeruginosa and Candida albicans. The improved analogues displayed no significant toxicity against human cells, and thus, KR-12 is a tuneable template for antibiotic development.

Ort, förlag, år, upplaga, sidor
WILEY-V C H VERLAG GMBH, 2018
Nyckelord
antibiotics, cytotoxicity, drug discovery, peptides, structure-activity relationships
Nationell ämneskategori
Biokemi och molekylärbiologi
Identifikatorer
urn:nbn:se:uu:diva-356391 (URN)10.1002/cbic.201700599 (DOI)000431625100008 ()29430821 (PubMedID)
Forskningsfinansiär
Vetenskapsrådet, 2011-3403Carl Tryggers stiftelse för vetenskaplig forskning , CTS 10: 126Carl Tryggers stiftelse för vetenskaplig forskning , CTS 11: 169Svenska läkaresällskapet, SLS-254511
Tillgänglig från: 2018-07-25 Skapad: 2018-07-25 Senast uppdaterad: 2020-02-18Bibliografiskt granskad
Nyström, L., Al-Rammahi, N., Malekkhaiat Häffner, S., Strömstedt, A. A., Browning, K. L. & Malmsten, M. (2018). Avidin-biotin cross-linked microgel multilayers as carriers for antimicrobial peptides. Biomacromolecules, 19(12), 4691-4702
Öppna denna publikation i ny flik eller fönster >>Avidin-biotin cross-linked microgel multilayers as carriers for antimicrobial peptides
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2018 (Engelska)Ingår i: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 19, nr 12, s. 4691-4702Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Herein, we report on the formation of cross-linked antimicrobial peptide-loaded microgel multilayers. Poly(ethyl acrylate- co-methacrylic acid) microgels were synthesized and functionalized with biotin to enable the formation of microgel multilayers cross-linked with avidin. Microgel functionalization and avidin cross-linking were verified with infrared spectroscopy, dynamic light scattering, and z-potential measurements, while multilayer formation (up to four layers) was studied with null ellipsometry and quartz crystal microbalance with dissipation (QCM-D). Incorporation of the antimicrobial peptide KYE28 (KYEITTIHNLFRKLTHRLFRRNFGYTLR) into the microgel multilayers was achieved either in one shot after multilayer formation or through addition after each microgel layer deposition. The latter was found to strongly promote peptide incorporation. Further, antimicrobial properties of the peptide-loaded microgel multilayers against Escherichia coli were investigated and compared to those of a peptide-loaded microgel monolayer. Results showed a more pronounced suppression in bacterial viability in suspension for the microgel multilayers. Correspondingly, LIVE/DEAD staining showed promoted disruption of adhered bacteria for the KYE28-loaded multilayers. Taken together, cross-linked microgel multilayers thus show promise as high load surface coatings for antimicrobial peptides.

Nationell ämneskategori
Farmaceutiska vetenskaper
Forskningsämne
Farmaceutisk fysikalisk kemi
Identifikatorer
urn:nbn:se:uu:diva-361399 (URN)10.1021/acs.biomac.8b01484 (DOI)000453109200018 ()
Forskningsfinansiär
Vetenskapsrådet, 2016-05157
Tillgänglig från: 2018-09-24 Skapad: 2018-09-24 Senast uppdaterad: 2019-01-15Bibliografiskt granskad
Abdillahi, S. M., Maass, T., Kasetty, G., Strömstedt, A. A., Baumgarten, M., Tati, R., . . . Mörgelin, M. (2018). Collagen VI Contains Multiple Host Defense Peptides with Potent In Vivo Activity. Journal of Immunology, 201(3), 1007-1020
Öppna denna publikation i ny flik eller fönster >>Collagen VI Contains Multiple Host Defense Peptides with Potent In Vivo Activity
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2018 (Engelska)Ingår i: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 201, nr 3, s. 1007-1020Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Collagen VI is a ubiquitous extracellular matrix component that forms extensive microfibrillar networks in most connective tissues. In this study, we describe for the first time, to our knowledge, that the collagen VI von Willebrand factor type A like domains exhibit a broad-spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria in human skin infections in vivo. In silico sequence and structural analysis of VWA domains revealed that they contain cationic and amphipathic peptide sequence motifs, which might explain the antimicrobial nature of collagen VI. In vitro and in vivo studies show that these peptides exhibited significant antibacterial activity against Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa through membrane disruption. Our findings shed new light on the role of collagen VI derived peptides in innate host defense and provide templates for development of peptide-based antibacterial therapies.

Ort, förlag, år, upplaga, sidor
AMER ASSOC IMMUNOLOGISTS, 2018
Nationell ämneskategori
Immunologi inom det medicinska området
Identifikatorer
urn:nbn:se:uu:diva-364467 (URN)10.4049/jimmunol.1700602 (DOI)000443582200019 ()29925677 (PubMedID)
Forskningsfinansiär
Stiftelsen för strategisk forskning (SSF), SB12-0019Vetenskapsrådet, 7480Crafoordska stiftelsenDeutsche Forschungsgemeinschaft (DFG), SFB829
Tillgänglig från: 2018-10-31 Skapad: 2018-10-31 Senast uppdaterad: 2018-10-31Bibliografiskt granskad
Slazak, B., Kapusta, M., Strömstedt, A. A., Slomka, A., Krychowiak, M., Shariatgorji, M., . . . Göransson, U. (2018). How Does the Sweet Violet (Viola odorata L.) Fight Pathogens and Pests - Cyclotides as a Comprehensive Plant Host Defense System. Frontiers in Plant Science, 9, Article ID 1296.
Öppna denna publikation i ny flik eller fönster >>How Does the Sweet Violet (Viola odorata L.) Fight Pathogens and Pests - Cyclotides as a Comprehensive Plant Host Defense System
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2018 (Engelska)Ingår i: Frontiers in Plant Science, ISSN 1664-462X, E-ISSN 1664-462X, Vol. 9, artikel-id 1296Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Cyclotides are cyclic plant polypeptides of 27-37 amino acid residues. They have been extensively studied in bioengineering and drug development contexts. However, less is known about the relevance of cyclotides for the plants producing them. The anti-insect larvae effects of kB1 and antibacterial activity of cyO2 suggest that cyclotides are a part of plant host defense. The sweet violet (Viola odorata L.) produces a wide array of cyclotides, including kB1 (kalata B1) and cyO2 (cycloviolacin O2), with distinct presumed biological roles. Here, we evaluate V. odorata cyclotides' potency against plant pathogens and their mode of action using bioassays, liposome experiments and immunogold labeling for transmission electron microscopy (TEM). We explore the link between the biological activity and distribution in plant generative, vegetative tissues and seeds, depicted by immunohistochemistry and matrix assisted laser desorption ionization mass spectrometry imaging (MALDI-MSI). Cyclotides cyO2, cyO3, cyO13, and cyO19 are shown to have potent activity against model fungal plant pathogens (Fusarium oxysporum, F. graminearum, F. culmorum, Mycosphaerella fragariae, Botrytis cinerea) and fungi isolated from violets (Colletotrichum utrechtense and Alternaria alternata), with minimal inhibitory concentrations (MICs) ranging from 0.8 to 25 mu M. Inhibition of phytopathogenic bacteria - Pseudomonas syringae pv. syringae, Dickeya dadantii and Pectobacterium atrosepticum - is also observed with MIC = 25-100 mu M. A membrane-disrupting antifungal mode of action is shown. Finding cyO2 inside the fungal spore cells in TEM images may indicate that other, intracellular targets may be involved in the mechanism of toxicity. Fungi can not break down cyclotides in the course of days. varv A (kalata S) and kB1 show little potency against pathogenic fungi when compared with the tested cycloviolacins. cyO2, cyO3, cyO19 and kB1 are differentially distributed and found in tissues vulnerable to pathogen (epidermis, rizodermis, vascular bundles, protodermis, procambium, ovary walls, outer integuments) and pest ( ground tissues of leaf and petiole) attacks, respectively, indicating a link between the cyclotides' sites of accumulation and biological role. Cyclotides emerge as a comprehensive defense system in V. odorata, in which different types of peptides have specific targets that determine their distribution in plant tissues.

Ort, förlag, år, upplaga, sidor
FRONTIERS MEDIA SA, 2018
Nyckelord
cyclotides, plant host defense, Violaceae, antimicrobial peptide, antifungal defense, MALDI-MSI, immunohistochemistry
Nationell ämneskategori
Botanik
Identifikatorer
urn:nbn:se:uu:diva-365299 (URN)10.3389/fpls.2018.01296 (DOI)000444243600001 ()30254654 (PubMedID)
Forskningsfinansiär
Vetenskapsrådet, 621-2007-5167Vetenskapsrådet, 621-2014-6215Stiftelsen för strategisk forskning (SSF), RIF14-0078Science for Life Laboratory - a national resource center for high-throughput molecular bioscience
Tillgänglig från: 2018-11-13 Skapad: 2018-11-13 Senast uppdaterad: 2018-11-13Bibliografiskt granskad
Nyström, L., Strömstedt, A. A., Schmidtchen, A. & Malmsten, M. (2018). Peptide-Loaded Microgels as Antimicrobial and Anti-Inflammatory Surface Coatings. Biomacromolecules, 19(8), 3456-3466
Öppna denna publikation i ny flik eller fönster >>Peptide-Loaded Microgels as Antimicrobial and Anti-Inflammatory Surface Coatings
2018 (Engelska)Ingår i: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 19, nr 8, s. 3456-3466Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Here we report on covalently immobilized poly(ethyl acrylate- co-methacrylic acid) microgels loaded with the host defense peptide KYE28 (KYEITTIHNLFRKLTHRLFRRNFGYTLR), which is derived from human heparin cofactor II, as well as its poly(ethylene glycol)-conjugated (PEGylated) version, KYE28PEG. Peptide loading and release, as well as the consequences of these processes on the microgel and peptide properties, were studied by in situ ellipsometry, confocal microscopy, zeta potential measurements, and circular dichroism spectroscopy. The results show that the microgel-peptide interactions are electrostatically dominated, thus promoted at higher microgel charge density, while PEGylation suppresses peptide binding. PEGylation also enhances the α-helix induction observed for KYE28 upon microgel incorporation. Additionally, peptide release is facilitated at physiological salt concentration, particularly so for KYE28PEG, which illustrates the importance of electrostatic interactions. In vitro studies on Escherichia coli show that the microgel-modified surfaces display potent antifouling properties in both the absence and presence of the incorporated peptide. While contact killing dominates at low ionic strength for the peptide-loaded microgels, released peptides also provide antimicrobial activity in bulk at a high ionic strength. Additionally, KYE28- and KYE28PEG-loaded microgels display anti-inflammatory effects on human monocytes. Taken together, these results not only show that surface-bound microgels offer an interesting approach for local drug delivery of host defense peptides but also illustrate the need to achieve high surface loads of peptides for efficient biological effects.

Ort, förlag, år, upplaga, sidor
American Chemical Society (ACS), 2018
Nationell ämneskategori
Farmakologi och toxikologi Biomaterialvetenskap
Identifikatorer
urn:nbn:se:uu:diva-358186 (URN)10.1021/acs.biomac.8b00776 (DOI)000441852400029 ()29976055 (PubMedID)
Forskningsfinansiär
Vetenskapsrådet, 2016-05157 2017-02341
Tillgänglig från: 2018-08-24 Skapad: 2018-08-24 Senast uppdaterad: 2018-11-06Bibliografiskt granskad
Nyström, L., Nordström, R., Strömstedt, A. A., Saunders, B., Alvarez-Asencio, R., Rutland, M. & Malmsten, M. (2018). Peptide-loaded microgels as antimicrobial surface coatings. Paper presented at 255th National Meeting and Exposition of the American-Chemical-Society (ACS) - Nexus of Food, Energy, and Water, MAR 18-22, 2018, New Orleans, LA. Abstract of Papers of the American Chemical Society, 255
Öppna denna publikation i ny flik eller fönster >>Peptide-loaded microgels as antimicrobial surface coatings
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2018 (Engelska)Ingår i: Abstract of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 255Artikel i tidskrift, Meeting abstract (Övrigt vetenskapligt) Published
Nationell ämneskategori
Fysikalisk kemi
Identifikatorer
urn:nbn:se:uu:diva-367230 (URN)000435539907572 ()
Konferens
255th National Meeting and Exposition of the American-Chemical-Society (ACS) - Nexus of Food, Energy, and Water, MAR 18-22, 2018, New Orleans, LA
Tillgänglig från: 2018-12-06 Skapad: 2018-12-06 Senast uppdaterad: 2018-12-06Bibliografiskt granskad
Organisationer
Identifikatorer
ORCID-id: ORCID iD iconorcid.org/0000-0001-9070-6944

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