Change search
Link to record
Permanent link

Direct link
BETA
Publications (10 of 12) Show all publications
Lindgren, J. F., Ytreberg, E., Holmqvist, A., Dahlström, M., Dahl, P., Berglin, M., . . . Dahlström, M. (2018). Copper release rate needed to inhibit fouling on the west coast of Sweden and control of copper release using zinc oxide. Biofouling (Print), 34(4), 453
Open this publication in new window or tab >>Copper release rate needed to inhibit fouling on the west coast of Sweden and control of copper release using zinc oxide
Show others...
2018 (English)In: Biofouling (Print), ISSN 0892-7014, E-ISSN 1029-2454, Vol. 34, no 4, p. 453-Article in journal (Refereed) Published
Abstract [en]

How zinc oxide influences copper release has been tested and the lowest release rate of copper from various combinations of copper and zinc in a paint matrix evaluated, whilst still deterring macrofouling, including barnacles and bryozoans. Copper (I) oxide was added to a generic AF paint in 0, 8.5, 11.7 or 16.3 wt% copper oxide in combination with 0, 10 or 20 wt% zinc oxide and applied on PMMA panels. The results show that zinc influences the release rate of copper. When 10 and 20 wt% zinc was added, the total amount of copper released significantly increased by on average 32 and 47% respectively. All treatments that included copper were successful in deterring macrofouling, including the treatment with the lowest average Cu release rate, ie 4.68 μg cm−2 day−1. 

Keywords
antifouling, Biofouling, copper, release rate, X-ray fluorescence, zinc
National Category
Natural Sciences
Identifiers
urn:nbn:se:ri:diva-33883 (URN)10.1080/08927014.2018.1463523 (DOI)2-s2.0-85047132640 (Scopus ID)
Available from: 2018-05-30 Created: 2018-05-30 Last updated: 2018-12-12Bibliographically approved
Pansch, C., Jonsson, P. R., Berglin, M., Pinori, E. & Wrange, A.-L. (2017). A new flow-through bioassay for testing low-emission antifouling coatings. Biofouling (Print), 33(8), 613-623
Open this publication in new window or tab >>A new flow-through bioassay for testing low-emission antifouling coatings
Show others...
2017 (English)In: Biofouling (Print), ISSN 0892-7014, E-ISSN 1029-2454, Vol. 33, no 8, p. 613-623Article in journal (Refereed) Published
Abstract [en]

Current antifouling (AF) technologies are based on the continuous release of biocides into the water, and consequently discharge into the environment. Major efforts to develop more environmentally friendly coatings require efficient testing in laboratory assays, followed by field studies. Barnacles are important fouling organisms worldwide, increasing hydrodynamic drag on ships and damaging coatings on underwater surfaces, and thus are extensively used as models in AF research, mostly in static, laboratory-based systems. Reliable flow-through test assays for the screening of biocide-containing AF paints, however, are rare. Herein, a flow-through bioassay was developed to screen for diverse low-release biocide paints, and to evaluate their effects on pre- and post-settlement traits in barnacles. The assay distinguishes between the effects from direct surface contact and bulk-water effects, which are crucial when developing low-emission AF coatings. This flow-through bioassay adds a new tool for rapid laboratory-based first-stage screening of candidate compounds and novel AF formulations.

Keywords
abamectin, antifouling assay, Balanus (Amphibalanus) improvisus, copper, low-release/emission coatings, static vs flow-through
National Category
Natural Sciences
Identifiers
urn:nbn:se:ri:diva-30820 (URN)10.1080/08927014.2017.1349897 (DOI)2-s2.0-85027128607 (Scopus ID)
Available from: 2017-09-06 Created: 2017-09-06 Last updated: 2019-02-05Bibliographically approved
Fromell, K., Yang, Y., Nilsson Ekdahl, K., Nilsson, B., Berglin, M. & Elwing, H. (2017). Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility. Biointerphases, 12(2), Article ID 02D417.
Open this publication in new window or tab >>Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility
Show others...
2017 (English)In: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 12, no 2, article id 02D417Article in journal (Refereed) Published
Abstract [en]

In previous investigations, the authors have examined the adsorption of albumin, immunoglobulin, and fibrinogen to a series of acrylate polymers with different backbone and side-group flexibility. The authors showed that protein adsorption to acrylates with high flexibility, such as poly(lauryl methacrylate) (PLMA), tends to preserve native conformation. In the present study, the authors have continued this work by examining the conformational changes that occur during the binding of complement factor 3 (C3) and coagulation factor XII (FXII). Native C3 adsorbed readily to all solid surfaces tested, including a series of acrylate surfaces of varying backbone flexibility. However, a monoclonal antibody recognizing a "hidden" epitope of C3 (only exposed during C3 activation or denaturation) bound to the C3 on the rigid acrylate surfaces or on polystyrene (also rigid), but not to C3 on the flexible PLMA, indicating that varying degrees of conformational change had occurred with binding to different surfaces. Similarly, FXII was activated only on the rigid poly(butyl methacrylate) surface, as assessed by the formation of FXIIa-antithrombin (AT) complexes; in contrast, it remained in its native form on the flexible PLMA surface. The authors also found that water wettability hysteresis, defined as the difference between the advancing and receding contact angles, was highest for the PLMA surface, indicating that a dynamic change in the interface polymer structure may help protect the adsorbed protein from conformational changes and denaturation.

National Category
Natural Sciences
Identifiers
urn:nbn:se:ri:diva-30900 (URN)10.1116/1.4985698 (DOI)2-s2.0-85021073944 (Scopus ID)
Note

 Funding details: VR, Vetenskapsrådet; Funding text: The authors wish to thank Deborah McClellan for much appreciated editorial assistance and the authors appreciate Pentti Tengvall for valuable discussions during the preparation of this work. This work was supported by grants from the European Community's Seventh Framework Program under Grant Agreement No. 602699 (DIREKT), the Swedish Research Council (VR), and faculty grants from the Linnaeus University.

Available from: 2017-09-06 Created: 2017-09-06 Last updated: 2018-12-19Bibliographically approved
Lundgren, A., Munktell, S., Lacey, M., Berglin, M. & Björefors, F. (2016). Formation of gold nanoparticle size and density gradients via bipolar electrochemistry. ChemElectroChem, 3(3), 378-382
Open this publication in new window or tab >>Formation of gold nanoparticle size and density gradients via bipolar electrochemistry
Show others...
2016 (English)In: ChemElectroChem, ISSN 2196-0216, Vol. 3, no 3, p. 378-382Article in journal (Refereed) Published
Abstract [en]

Bipolar electrochemistry is employed to demonstrate the formation of gold nanoparticle size gradients on planar surfaces. By controlling the electric field in a HAuCl4-containing electrolyte, gold was reduced onto 10nm diameter particles immobilized on pre-modified thiolated bipolar electrode (BPE) templates, resulting in larger particles towards the more cathodic direction. As the gold deposition was the dominating cathodic reaction, the increased size of the nanoparticles also reflected the current distribution on the bipolar electrode. The size gradients were also combined with a second gradient-forming technique to establish nanoparticle surfaces with orthogonal size and density gradients, resulting in a wide range of combinations of small/large and few/many particles on a single bipolar electrode. Such surfaces are valuable in, for example, cell-material interaction and combinatorial studies, where a large number of conditions are probed simultaneously.

Place, publisher, year, edition, pages
Wiley-VCH Verlagsgesellschaft, 2016
Keywords
Bipolar electrochemistry, Gold nanoparticles, Interfaces, Size gradients, Templated deposition
National Category
Materials Chemistry Physical Chemistry
Identifiers
urn:nbn:se:ri:diva-89 (URN)10.1002/celc.201500413 (DOI)2-s2.0-84960193104 (Scopus ID)
Available from: 2016-05-24 Created: 2016-04-28 Last updated: 2019-06-14Bibliographically approved
Dahlström, M., Sjögren, M., Jonsson, P. R., Göransson, U., Lindh, L., Arnebrant, T., . . . Berglin, M. (2015). Affinity states of biocides determine bioavailability and release rates in marine paints (ed.). Biofouling (Print), 31(2), 201-210
Open this publication in new window or tab >>Affinity states of biocides determine bioavailability and release rates in marine paints
Show others...
2015 (English)In: Biofouling (Print), ISSN 0892-7014, E-ISSN 1029-2454, Vol. 31, no 2, p. 201-210Article in journal (Refereed) Published
Abstract [en]

A challenge for the next generation marine antifouling (AF) paints is to deliver minimum amounts of biocides to the environment. The candidate AF compound medetomidine is here shown to be released at very low concentrations, ie ng ml(-1) day(-1). Moreover, the release rate of medetomidine differs substantially depending on the formulation of the paint, while inhibition of barnacle settlement is independent of release to the ambient water, ie the paint with the lowest release rate was the most effective in impeding barnacle colonisation. This highlights the critical role of chemical interactions between biocide, paint carrier and the solid/aqueous interface for release rate and AF performance. The results are discussed in the light of differential affinity states of the biocide, predicting AF activity in terms of a high surface affinity and preserved bioavailability. This may offer a general framework for the design of low-release paint systems using biocides for protection against biofouling on marine surfaces.

Keywords
Antifouling biocides, Barnacle, Ellipsometry, Release, RP-HPLC, Surface adsorption
National Category
Natural Sciences
Identifiers
urn:nbn:se:ri:diva-6828 (URN)10.1080/08927014.2015.1012639 (DOI)25775096 (PubMedID)23625 (Local ID)23625 (Archive number)23625 (OAI)
Available from: 2016-09-08 Created: 2016-09-08 Last updated: 2019-07-02Bibliographically approved
Berglin, M. (2014). Gold-nanoparticle-assisted self-assembly of chemical gradients with tunable sub-50 nm molecular domains (ed.). Particle & particle systems characterization, 31(2), 209-218
Open this publication in new window or tab >>Gold-nanoparticle-assisted self-assembly of chemical gradients with tunable sub-50 nm molecular domains
2014 (English)In: Particle & particle systems characterization, ISSN 0934-0866, E-ISSN 1521-4117, Vol. 31, no 2, p. 209-218Article in journal (Refereed) Published
Abstract [en]

A simple and efficient principle for nanopatterning with wide applicability in the sub-50 nanometer regime is chemisorption of nanoparticles; at homogeneous substrates, particles carrying surface charge may spontaneously self-organize due to the electrostatic repulsion between adjacent particles. Guided by this principle, a method is presented to design, self-assemble, and chemically functionalize gradient nanopatterns where the size of molecular domains can be tuned to match the level corresponding to single protein binding events. To modulate the binding of negatively charged gold nanoparticles both locally (<100 nm) and globally (>100 μm) onto a single modified gold substrate, ion diffusion is used to achieve spatial control of the particles' mutual electrostatic interactions. By subsequent tailoring of different molecules to surface-immobilized particles and the void areas surrounding them, nanopatterns are obtained with variable chemical domains along the gradient surface. Fimbriated Escherichia coli bacteria are bound to gradient nanopatterns with similar molecular composition and macroscopic contact angle, but different sizes of nanoscopic presentation of adhesive (hydrophobic) and repellent poly(ethylene) glycol (PEG) domains. It is shown that small hydrophobic domains, similar in size to the diameter of the bacterial fimbriae, supported firmly attached bacteria resembling catch-bond binding, whereas a high number of loosely adhered bacteria are observed on larger hydrophobic domains. Chemical gradients with the resolution needed to address complex biological binding events at the single protein level are prepared using surface-deposited gold nanoparticles as a versatile template for orthogonal chemicalmodifications. The effect of hydrophobic domain arrangement on the sub-50 nm scale is shown to influence binding of fimbriae carrying E. coli bacteria. 

National Category
Natural Sciences
Identifiers
urn:nbn:se:ri:diva-6711 (URN)10.1002/ppsc.201300154 (DOI)2-s2.0-84893984535 (Scopus ID)23710 (Local ID)23710 (Archive number)23710 (OAI)
Available from: 2016-09-08 Created: 2016-09-08 Last updated: 2019-08-14Bibliographically approved
Trepos, R., Pinori, E., Jonsson, P. R., Berglin, M., Svenson, J. & Coutinho, R. (2014). Innovative approaches for the development of new copper-free marine antifouling paints (ed.). Journal of Ship and Ocean Technology, 9(4), 7-18
Open this publication in new window or tab >>Innovative approaches for the development of new copper-free marine antifouling paints
Show others...
2014 (English)In: Journal of Ship and Ocean Technology, ISSN 1226-5594, Vol. 9, no 4, p. 7-18Article in journal (Refereed) Published
National Category
Natural Sciences
Identifiers
urn:nbn:se:ri:diva-27043 (URN)
Note

A3400

Available from: 2016-12-08 Created: 2016-12-08 Last updated: 2018-08-13Bibliographically approved
Berglin, M. (2013). Gradients in surface nanotopography used to study platelet adhesion and activation (ed.). Colloids and Surfaces B: Biointerfaces, 110(1), 261-269
Open this publication in new window or tab >>Gradients in surface nanotopography used to study platelet adhesion and activation
2013 (English)In: Colloids and Surfaces B: Biointerfaces, ISSN 0927-7765, E-ISSN 1873-4367, Vol. 110, no 1, p. 261-269Article in journal (Refereed) Published
National Category
Natural Sciences
Identifiers
urn:nbn:se:ri:diva-6572 (URN)23865 (Local ID)23865 (Archive number)23865 (OAI)
Available from: 2016-09-08 Created: 2016-09-08 Last updated: 2018-08-13Bibliographically approved
Berglin, M. (2013). Pellet formation of zygomycetes and immobilization of yeast (ed.). New Biotechnology, 30(5), 516-522
Open this publication in new window or tab >>Pellet formation of zygomycetes and immobilization of yeast
2013 (English)In: New Biotechnology, ISSN 1871-6784, E-ISSN 1876-4347, Vol. 30, no 5, p. 516-522Article in journal (Refereed) Published
National Category
Natural Sciences
Identifiers
urn:nbn:se:ri:diva-6548 (URN)23831 (Local ID)23831 (Archive number)23831 (OAI)
Available from: 2016-09-08 Created: 2016-09-08 Last updated: 2018-08-13Bibliographically approved
Pinori, E. & Berglin, M. (2013). The impact of coating hardness on the anti-barnacle efficacy of an embedded antifouling biocide (ed.). Biofouling (Print), 29(7), 763-773
Open this publication in new window or tab >>The impact of coating hardness on the anti-barnacle efficacy of an embedded antifouling biocide
2013 (English)In: Biofouling (Print), ISSN 0892-7014, E-ISSN 1029-2454, Vol. 29, no 7, p. 763-773Article in journal (Refereed) Published
National Category
Natural Sciences
Identifiers
urn:nbn:se:ri:diva-6544 (URN)23825 (Local ID)23825 (Archive number)23825 (OAI)
Available from: 2016-09-08 Created: 2016-09-08 Last updated: 2018-08-13Bibliographically approved
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-9377-8924

Search in DiVA

Show all publications
v. 2.35.7