uu.seUppsala University Publications
Change search
Link to record
Permanent link

Direct link
BETA
Strömstedt, Adam A., DocentORCID iD iconorcid.org/0000-0001-9070-6944
Alternative names
Publications (10 of 33) Show all publications
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.
Open this publication in new window or tab >>Antimicrobial function of short amidated peptide fragments from the tick-derived OsDef2 defensin.
Show others...
2019 (English)In: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 25, no 12, article id e3223Article in journal (Refereed) 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.

Keywords
antimicrobial resistance, carboxyamidation, mechanism of action, membrane permeabilization, minimalized peptide, tick defensin
National Category
Medicinal Chemistry
Identifiers
urn:nbn:se:uu:diva-401412 (URN)10.1002/psc.3223 (DOI)31713951 (PubMedID)
Available from: 2020-01-07 Created: 2020-01-07 Last updated: 2020-02-05Bibliographically approved
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
Open this publication in new window or tab >>Nanoclay-induced bacterial flocculation for infection confinement
Show others...
2019 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 562, p. 71-80Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
Elsevier, 2019
Keywords
Antimicrobial, Bacteria flocculation, Infection confinement, Membrane
National Category
Pharmaceutical Sciences Medicinal Chemistry
Identifiers
urn:nbn:se:uu:diva-401401 (URN)10.1016/j.jcis.2019.11.110 (DOI)000508752700008 ()31837621 (PubMedID)
Funder
Swedish Research Council, 2016-05157
Available from: 2020-01-07 Created: 2020-01-07 Last updated: 2020-03-20Bibliographically approved
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.
Open this publication in new window or tab >>Screening for bioactive secondary metabolites in Sri Lankan medicinal plants by microfractionation and targeted isolation of antimicrobial flavonoids from Derris scandens
Show others...
2019 (English)In: Journal of Ethnopharmacology, ISSN 0378-8741, E-ISSN 1872-7573, Vol. 246, article id 112158Article in journal (Refereed) 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.

Keywords
Sri Lanka, Medicinal plants, Microfractionation, Antimicrobial activity, Cytotoxicity, Flavonoids
National Category
Pharmacology and Toxicology
Identifiers
urn:nbn:se:uu:diva-397136 (URN)10.1016/j.jep.2019.112158 (DOI)000493211800010 ()31421182 (PubMedID)
Funder
Swedish Research Council, 2013-06672
Available from: 2019-11-28 Created: 2019-11-28 Last updated: 2019-11-28Bibliographically approved
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.
Open this publication in new window or tab >>Action of antimicrobial peptides and their prodrugs on model and biological membranes
Show others...
2018 (English)In: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 24, no 7, article id e3086Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
WILEY, 2018
Keywords
antimicrobial peptides, liposomes, membrane permeabilization, prodrugs, therapeutic index
National Category
Pharmaceutical Sciences
Identifiers
urn:nbn:se:uu:diva-362847 (URN)10.1002/psc.3086 (DOI)000440144700002 ()29799150 (PubMedID)
Conference
7th International Meeting on Antimicrobial Peptides, AUG 25-27, 2017, Univ Copenhagen, Copenhagen, DENMARK
Available from: 2018-10-15 Created: 2018-10-15 Last updated: 2018-10-15Bibliographically approved
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
Open this publication in new window or tab >>Alanine and Lysine Scans of the LL-37-Derived Peptide Fragment KR-12 Reveal Key Residues for Antimicrobial Activity
Show others...
2018 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 19, no 9, p. 931-939Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
WILEY-V C H VERLAG GMBH, 2018
Keywords
antibiotics, cytotoxicity, drug discovery, peptides, structure-activity relationships
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:uu:diva-356391 (URN)10.1002/cbic.201700599 (DOI)000431625100008 ()29430821 (PubMedID)
Funder
Swedish Research Council, 2011-3403Carl Tryggers foundation , CTS 10: 126Carl Tryggers foundation , CTS 11: 169Swedish Society of Medicine, SLS-254511
Available from: 2018-07-25 Created: 2018-07-25 Last updated: 2020-02-18Bibliographically approved
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
Open this publication in new window or tab >>Avidin-biotin cross-linked microgel multilayers as carriers for antimicrobial peptides
Show others...
2018 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 19, no 12, p. 4691-4702Article in journal (Refereed) 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.

National Category
Pharmaceutical Sciences
Research subject
Pharmaceutical Physical Chemistry
Identifiers
urn:nbn:se:uu:diva-361399 (URN)10.1021/acs.biomac.8b01484 (DOI)000453109200018 ()
Funder
Swedish Research Council, 2016-05157
Available from: 2018-09-24 Created: 2018-09-24 Last updated: 2019-01-15Bibliographically approved
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
Open this publication in new window or tab >>Collagen VI Contains Multiple Host Defense Peptides with Potent In Vivo Activity
Show others...
2018 (English)In: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 201, no 3, p. 1007-1020Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
AMER ASSOC IMMUNOLOGISTS, 2018
National Category
Immunology in the medical area
Identifiers
urn:nbn:se:uu:diva-364467 (URN)10.4049/jimmunol.1700602 (DOI)000443582200019 ()29925677 (PubMedID)
Funder
Swedish Foundation for Strategic Research , SB12-0019Swedish Research Council, 7480The Crafoord FoundationGerman Research Foundation (DFG), SFB829
Available from: 2018-10-31 Created: 2018-10-31 Last updated: 2018-10-31Bibliographically approved
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.
Open this publication in new window or tab >>How Does the Sweet Violet (Viola odorata L.) Fight Pathogens and Pests - Cyclotides as a Comprehensive Plant Host Defense System
Show others...
2018 (English)In: Frontiers in Plant Science, ISSN 1664-462X, E-ISSN 1664-462X, Vol. 9, article id 1296Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
FRONTIERS MEDIA SA, 2018
Keywords
cyclotides, plant host defense, Violaceae, antimicrobial peptide, antifungal defense, MALDI-MSI, immunohistochemistry
National Category
Botany
Identifiers
urn:nbn:se:uu:diva-365299 (URN)10.3389/fpls.2018.01296 (DOI)000444243600001 ()30254654 (PubMedID)
Funder
Swedish Research Council, 621-2007-5167Swedish Research Council, 621-2014-6215Swedish Foundation for Strategic Research , RIF14-0078Science for Life Laboratory - a national resource center for high-throughput molecular bioscience
Available from: 2018-11-13 Created: 2018-11-13 Last updated: 2018-11-13Bibliographically approved
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
Open this publication in new window or tab >>Peptide-Loaded Microgels as Antimicrobial and Anti-Inflammatory Surface Coatings
2018 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 19, no 8, p. 3456-3466Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018
National Category
Pharmacology and Toxicology Biomaterials Science
Identifiers
urn:nbn:se:uu:diva-358186 (URN)10.1021/acs.biomac.8b00776 (DOI)000441852400029 ()29976055 (PubMedID)
Funder
Swedish Research Council, 2016-05157 2017-02341
Available from: 2018-08-24 Created: 2018-08-24 Last updated: 2018-11-06Bibliographically approved
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
Open this publication in new window or tab >>Peptide-loaded microgels as antimicrobial surface coatings
Show others...
2018 (English)In: Abstract of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 255Article in journal, Meeting abstract (Other academic) Published
National Category
Physical Chemistry
Identifiers
urn:nbn:se:uu:diva-367230 (URN)000435539907572 ()
Conference
255th National Meeting and Exposition of the American-Chemical-Society (ACS) - Nexus of Food, Energy, and Water, MAR 18-22, 2018, New Orleans, LA
Available from: 2018-12-06 Created: 2018-12-06 Last updated: 2018-12-06Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0001-9070-6944

Search in DiVA

Show all publications