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Arnebrant, Thomas
Publications (10 of 108) Show all publications
Gonzalez-Martinez, J. F., Boyd, H., Gutfreund, P., Welbourn, R. J., Robertsson, C., Wickström, C., . . . Sotres, J. (2022). MUC5B mucin films under mechanical confinement: A combined neutron reflectometry and atomic force microscopy study.. Journal of Colloid and Interface Science, 614, 120-129, Article ID S0021-9797(22)00109-6.
Open this publication in new window or tab >>MUC5B mucin films under mechanical confinement: A combined neutron reflectometry and atomic force microscopy study.
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2022 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 614, p. 120-129, article id S0021-9797(22)00109-6Article in journal (Refereed) Published
Abstract [en]

HYPOTHESIS: Among other functions, mucins hydrate and protect biological interfaces from mechanical challenges. Mucins also attract interest as biocompatible coatings with excellent lubrication performance. Therefore, it is of high interest to understand the structural response of mucin films to mechanical challenges. We hypothesized that this could be done with Neutron Reflectometry using a novel sample environment where mechanical confinement is achieved by inflating a membrane against the films.

EXPERIMENTS: Oral MUC5B mucin films were investigated by Force Microscopy/Spectroscopy and Neutron Reflectometry both at solid-liquid interfaces and under mechanical confinement.

FINDINGS: NR indicated that MUC5B films were almost completely compressed and dehydrated when confined at 1 bar. This was supported by Force Microscopy/Spectroscopy investigations. Force Spectroscopy also indicated that MUC5B films could withstand mechanical confinement by means of steric interactions for pressures lower than ∼ 0.5 bar i.e., mucins could protect interfaces from mechanical challenges of this magnitude while keeping them hydrated. To investigate mucin films under these pressures by means of the employed sample environment for NR, further technological developments are needed. The most critical would be identifying or developing more flexible membranes that would still meet certain requirements like chemical homogeneity and very low roughness.

Place, publisher, year, edition, pages
Elsevier, 2022
Keywords
Atomic force microscopy, Force spectroscopy, Mechanical confinement, Mucins, Neutron reflectometry
National Category
Physical Chemistry
Identifiers
urn:nbn:se:mau:diva-50061 (URN)10.1016/j.jcis.2022.01.096 (DOI)000750672100013 ()35091141 (PubMedID)2-s2.0-85123366668 (Scopus ID)
Available from: 2022-02-09 Created: 2022-02-09 Last updated: 2024-02-05Bibliographically approved
Boyd, H., Gonzalez-Martinez, J. F., Welbourn, R. J., Gutfreund, P., Klechikov, A., Robertsson, C., . . . Sotres, J. (2021). A comparison between the structures of reconstituted salivary pellicles and oral mucin (MUC5B) films.. Journal of Colloid and Interface Science, 584, 660-668, Article ID S0021-9797(20)31464-8.
Open this publication in new window or tab >>A comparison between the structures of reconstituted salivary pellicles and oral mucin (MUC5B) films.
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2021 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 584, p. 660-668, article id S0021-9797(20)31464-8Article in journal (Refereed) Published
Abstract [en]

HYPOTHESIS: Salivary pellicles i.e., thin films formed upon selective adsorption of saliva, protect oral surfaces against chemical and mechanical insults. Pellicles are also excellent aqueous lubricants. It is generally accepted that reconstituted pellicles have a two-layer structure, where the outer layer is mainly composed of MUC5B mucins. We hypothesized that by comparing the effect of ionic strength on reconstituted pellicles and MUC5B films we could gain further insight into the pellicle structure.

EXPERIMENTS: Salivary pellicles and MUC5B films reconstituted on solid surfaces were investigated at different ionic strengths by Force Spectroscopy, Quartz Crystal Microbalance with Dissipation, Null Ellipsometry and Neutron Reflectometry.

FINDINGS: Our results support the two-layer structure for reconstituted salivary pellicles. The outer layer swelled when ionic strength decreased, indicating a weak polyelectrolyte behavior. While initially the MUC5B films exhibited a similar tendency, this was followed by a drastic collapse indicating an interaction between exposed hydrophobic domains. This suggests that mucins in the pellicle outer layer form complexes with other salivary components that prevent this interaction. Lowering ionic strength below physiological values also led to a partial removal of the pellicle inner layer. Overall, our results highlight the importance that the interactions of mucins with other pellicle components play on their structure.

Place, publisher, year, edition, pages
Elsevier, 2021
Keywords
Ionic strength, MUC5B, Mucin, Salivary pellicle, Steric forces
National Category
Dentistry
Identifiers
urn:nbn:se:mau:diva-37667 (URN)10.1016/j.jcis.2020.10.124 (DOI)000600220000006 ()33198975 (PubMedID)2-s2.0-85096107333 (Scopus ID)
Available from: 2020-12-21 Created: 2020-12-21 Last updated: 2023-10-30Bibliographically approved
Boyd, H., Gonzalez-Martinez, J. F., Welbourn, R. J., Ma, K., Li, P., Gutfreund, P., . . . Sotres, J. (2021). Effect of nonionic and amphoteric surfactants on salivary pellicles reconstituted in vitro. Scientific Reports, 11(1), Article ID 12913.
Open this publication in new window or tab >>Effect of nonionic and amphoteric surfactants on salivary pellicles reconstituted in vitro
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2021 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 11, no 1, article id 12913Article in journal (Refereed) Published
Abstract [en]

Surfactants are important components of oral care products. Sodium dodecyl sulfate (SDS) is the most common because of its foaming properties, taste and low cost. However, the use of ionic surfactants, especially SDS, is related to several oral mucosa conditions. Thus, there is a high interest in using non-ionic and amphoteric surfactants as they are less irritant. To better understand the performance of these surfactants in oral care products, we investigated their interaction with salivary pellicles i.e., the proteinaceous films that cover surfaces exposed to saliva. Specifically, we focused on pentaethylene glycol monododecyl ether (C12E5) and cocamidopropyl betaine (CAPB) as model nonionic and amphoteric surfactants respectively, and investigated their interaction with reconstituted salivary pellicles with various surface techniques: Quartz Crystal Microbalance with Dissipation, Ellipsometry, Force Spectroscopy and Neutron Reflectometry. Both C12E5 and CAPB were gentler on pellicles than SDS, removing a lower amount. However, their interaction with pellicles differed. Our work indicates that CAPB would mainly interact with the mucin components of pellicles, leading to collapse and dehydration. In contrast, exposure to C12E5 had a minimal effect on the pellicles, mainly resulting in the replacement/solubilisation of some of the components anchoring pellicles to their substrate.

Place, publisher, year, edition, pages
Nature Publishing Group, 2021
National Category
Physical Chemistry
Identifiers
urn:nbn:se:mau:diva-44076 (URN)10.1038/s41598-021-92505-4 (DOI)000667261900001 ()34155330 (PubMedID)2-s2.0-85108451872 (Scopus ID)
Available from: 2021-06-23 Created: 2021-06-23 Last updated: 2024-02-05Bibliographically approved
Tchekwagep, P. M., Eminovski, J. H., Nanseu-Njiki, C. P., Ngameni, E., Arnebrant, T. & Ruzgas, T. (2020). Adsorption of Bovine Serum Albumin on Silver Nanoparticle Layer Deposited on Mercaptohexylpyridinium-Coated Quartz Crystal Microbalance with Dissipation Gold Electrode: Studied by Electrochemical Quartz Crystal Microbalance with Dissipation. Physica Status Solidi (a) applications and materials science, 217(13), Article ID 1900839.
Open this publication in new window or tab >>Adsorption of Bovine Serum Albumin on Silver Nanoparticle Layer Deposited on Mercaptohexylpyridinium-Coated Quartz Crystal Microbalance with Dissipation Gold Electrode: Studied by Electrochemical Quartz Crystal Microbalance with Dissipation
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2020 (English)In: Physica Status Solidi (a) applications and materials science, ISSN 1862-6300, E-ISSN 1862-6319, Vol. 217, no 13, article id 1900839Article in journal (Refereed) Published
Abstract [en]

Increasing use of silver nanoparticles (AgNPs) in different consumer products provokes interest in understanding interactions of AgNPs with biological molecules, e.g., proteins. The adsorption of AgNPs and bovine serum albumin (BSA) onto self-assembled monolayer of mercaptohexylpyridinium (MHP) on gold surface is described. A quartz crystal microbalance coupled with electrochemical measurements are used to study interactions between AgNPs and BSA. It is found that AgNPs adsorbed on MHP can be considered as highly elastic (stiff) film as the dissipation Delta D approximate to 0. Measurements of the mass loss and the increase in dissipation in parallel with the electrochemical oxidation/reduction of AgNPs shows that albumin adsorption on AgNPs highly diminish electrochemical Ag/AgCl conversion. The formation of a less rigid Ag layer than the original MHP-AgNPs film is also indicated. The 3D assemblies of nanostructures observed with scanning electron microscopy (SEM) reveal clustering of particles after the redox process.

Place, publisher, year, edition, pages
John Wiley & Sons, 2020
National Category
Analytical Chemistry
Identifiers
urn:nbn:se:mau:diva-13812 (URN)10.1002/pssa.201900839 (DOI)000510693400001 ()2-s2.0-85088057554 (Scopus ID)
Available from: 2020-03-17 Created: 2020-03-17 Last updated: 2024-02-05Bibliographically approved
Valldeperas, M., Salis, A., Barauskas, J., Tiberg, F., Arnebrant, T., Razumas, V., . . . Nylandert, T. (2019). Enzyme encapsulation in nanostructured self-assembled structures: Toward biofunctional supramolecular assemblies. Current Opinion in Colloid & Interface Science, 44, 130-142
Open this publication in new window or tab >>Enzyme encapsulation in nanostructured self-assembled structures: Toward biofunctional supramolecular assemblies
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2019 (English)In: Current Opinion in Colloid & Interface Science, ISSN 1359-0294, E-ISSN 1879-0399, Vol. 44, p. 130-142Article, review/survey (Refereed) Published
Abstract [en]

Enzymes have come into use for many new applications outside their natural biological environment, taking advantage of their high efficiency and selectivity as biocatalysts. Such new application often requires encapsulation to preserve the structure and activity of the enzyme, but also to regulate and control the activity. Here, we will discuss two types of encapsulation, soft matrices consisting of polar lipid liquid crystals and hard ordered mesoporous silica matrices. For both types of matrices, the challenge is to control the pore size of the matrices and the interaction with the matrix interface. Here, the polar lipid liquid crystals offer larger flexibility than silica, but on the other hand, it is considerably more sensitive to the environment.

Place, publisher, year, edition, pages
Elsevier, 2019
Keywords
Enzyme encapsulation, Enzyme activity, Pore size, Polar lipid liquid crystals, Cubic phase, Mesoporous silica
National Category
Physical Chemistry
Identifiers
urn:nbn:se:mau:diva-17256 (URN)10.1016/j.cocis.2019.09.007 (DOI)000506474700011 ()2-s2.0-85074691860 (Scopus ID)
Available from: 2020-05-13 Created: 2020-05-13 Last updated: 2024-02-05Bibliographically approved
Krikstolaityte, V., Hamit-Eminovski, J., Abariute, L., Niaura, G., Meskys, R., Arnebrant, T., . . . Ruzgas, T. (2019). Impact of molecular linker size on physicochemical properties of assembled gold nanoparticle mono-/multi-layers and their applicability for functional binding of biomolecules (ed.). Journal of Colloid and Interface Science, 543, 307-316
Open this publication in new window or tab >>Impact of molecular linker size on physicochemical properties of assembled gold nanoparticle mono-/multi-layers and their applicability for functional binding of biomolecules
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2019 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 543, p. 307-316Article in journal (Refereed) Published
Abstract [en]

In this work the impact of molecular inter-linker size on gold nanoparticle (AuNP) mono-/multilayer structural properties, density and homogeneity has been investigated. These characteristics are of great importance for functional binding of biomolecules. Positively charged high or low molecular weight inter-linkers, poly-L-lysine (PLL) or N-(6-mercapto)hexylpyridinium (MHP), were used to attach negatively charged AuNPs on a planar gold surface as well as to further interlink into a multilayer structure via layer-by-layer deposition. The inter-particle interaction within the assembled AuNP films was adjusted by the ionic strength in the AuNPs dispersions The AuNP layer density and structural/viscoelastic properties were evaluated by the quartz crystal microbalance with dissipation (QCM-D) technique. The validity of the commercial Voigt model, specifically developed for quantitative QCM-D data analysis of homogeneous viscoelastic films, was evaluated by a model independent analysis when comparing the assembled AuNP films with a homogeneous layer of a mucin from bovine submaxillary glands. Both AuNP mono- and multilayers, attached/interlinked via long flexible PLL molecules assembled to denser and more soft/viscous structures compared to those interlinked by short MHP compounds. Thus, PLL-interlinked AuNP mono-/multilayer structures were further investigated as a platform for laccase enzyme functional adsorption via qualitative assessment of bioelectrochemical characteristics of the enzyme. (C) 2019 Elsevier Inc. All rights reserved.

Place, publisher, year, edition, pages
Elsevier, 2019
Keywords
Poly-L-lysine, N-(6-mercaptohexyl)pyridinium, Gold nanoparticles, Layer-by-layer deposition, Biomolecule adsorption, Bio-electro-catalysis, Electrochemical-quartz crystal, microbalance with dissipation
National Category
Natural Sciences
Identifiers
urn:nbn:se:mau:diva-4428 (URN)10.1016/j.jcis.2019.02.048 (DOI)000462416900033 ()30825679 (PubMedID)2-s2.0-85062011660 (Scopus ID)30190 (Local ID)30190 (Archive number)30190 (OAI)
Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2024-03-27Bibliographically approved
Nylander, T., Arnebrant, T., Cárdenas, M., Bos, M. & Wilde, P. (2019). Protein/Emulsifier Interactions. In: Gerard L. Hasenhuettl, Richard W. Hartel (Ed.), Food Emulsifiers and Their Applications: (pp. 101-192). Springer
Open this publication in new window or tab >>Protein/Emulsifier Interactions
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2019 (English)In: Food Emulsifiers and Their Applications / [ed] Gerard L. Hasenhuettl, Richard W. Hartel, Springer, 2019, p. 101-192Chapter in book (Refereed)
Abstract [en]

An important consequence of protein-lipid interaction is the effect on stability of the protein in solution as well as on its behavior at interfaces. Here we will discuss key aspects of protein aggregation and unfolding as well as the effects of protein structure (random coil proteins versus globular) that are relevant for our understanding protein-lipid interaction. The main types of emulsifiers are the (1) aqueous soluble, surfactant type and (2) lipids with low aqueous solubility. The monomer concentration as defined by cmc is an important parameter for the soluble lipids. For emulsifiers with low aqueous solubility the emulsifier self-assembly structure and its properties control the interaction with proteins. We will therefore summarize the main features of lipid self-assembly. It also allows us to define different plausible scenarios and principles and models for factors that control the interactions in real food (and Pharmaceutical) systems. For the food applications the fate of the lipid during digestion is important and therefore we will discuss some aspects of enzyme-catalyzed lipolysis in terms of the structural evolution. New products and concepts of using protein/emulsifier interactions will be exemplified by illustrating how food nanotechnology possibly can be used for the delivery of functionality.

Place, publisher, year, edition, pages
Springer, 2019
National Category
Food Engineering
Identifiers
urn:nbn:se:mau:diva-64563 (URN)10.1007/978-3-030-29187-7_5 (DOI)2-s2.0-85149573838 (Scopus ID)978-3-030-29185-3 (ISBN)978-3-030-29187-7 (ISBN)
Available from: 2023-12-18 Created: 2023-12-18 Last updated: 2023-12-18Bibliographically approved
Larpant, N., Pham, A. D., Shafaat, A., Gonzalez-Martinez, J. F., Sotres, J., Sjöholm, J., . . . Ruzgas, T. (2019). Sensing by wireless reading Ag/AgCl redox conversion on RFID tag: universal, battery-less biosensor design (ed.). Scientific Reports, 9, Article ID 12948.
Open this publication in new window or tab >>Sensing by wireless reading Ag/AgCl redox conversion on RFID tag: universal, battery-less biosensor design
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2019 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 9, article id 12948Article in journal (Refereed) Published
Abstract [en]

Massive integration of biosensors into design of Internet-of-Things (IoT) is vital for progress of healthcare. However, the integration of biosensors is challenging due to limited availability of battery-less biosensor designs. In this work, a combination of nanomaterials for wireless sensing of biological redox reactions is described. The design exploits silver nanoparticles (AgNPs) as part of the RFID tag antenna. We demonstrate that a redox enzyme, particularly, horseradish peroxidase (HRP), can convert AgNPs into AgCl in the presence of its substrate, hydrogen peroxide. This strongly changes the impedance of the tag. The presented example exploits gold nanoparticle (AuNP)-assisted electron transfer (ET) between AgNPs and HRP. We show that AuNP is a vital intermediate for establishing rapid ET between the enzyme and AgNPs. As an example, battery-less biosensor-RFID tag designs for H2O2 and glucose are demonstrated. Similar battery-less sensors can be constructed to sense redox reactions catalysed by other oxidoreductase enzymes, their combinations, bacteria or other biological and even non-biological catalysts. In this work, a fast and general route for converting a high number of redox reaction based sensors into battery-less sensor-RFID tags is described.

Place, publisher, year, edition, pages
Nature Publishing Group, 2019
Keywords
Multidisciplinary Sciences
National Category
Natural Sciences
Identifiers
urn:nbn:se:mau:diva-3963 (URN)10.1038/s41598-019-49245-3 (DOI)000484984700023 ()31506441 (PubMedID)2-s2.0-85072038367 (Scopus ID)30524 (Local ID)30524 (Archive number)30524 (OAI)
Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2024-02-05Bibliographically approved
Maric, S., Lind, T. K., Raida, M. R., Bengtsson, E., Fredrikson, G. N., Rogers, S., . . . Cárdenas, M. (2019). Time-resolved small-angle neutron scattering as a probe for the dynamics of lipid exchange between human lipoproteins and naturally derived membranes (ed.). Scientific Reports, 9(1), Article ID 7591.
Open this publication in new window or tab >>Time-resolved small-angle neutron scattering as a probe for the dynamics of lipid exchange between human lipoproteins and naturally derived membranes
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2019 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 9, no 1, article id 7591Article in journal (Refereed) Published
Abstract [en]

Atherosclerosis is the main killer in the western world. Today's clinical markers include the total level of cholesterol and high-/low-density lipoproteins, which often fails to accurately predict the disease. The relationship between the lipid exchange capacity and lipoprotein structure should explain the extent by which they release or accept lipid cargo and should relate to the risk for developing atherosclerosis. Here, small-angle neutron scattering and tailored deuteration have been used to follow the molecular lipid exchange between human lipoprotein particles and cellular membrane mimics made of natural, "neutron invisible" phosphatidylcholines. We show that lipid exchange occurs via two different processes that include lipid transfer via collision and upon direct particle tethering to the membrane, and that high-density lipoprotein excels at exchanging the human-like unsaturated phosphatidylcholine. By mapping the specific lipid content and level of glycation/oxidation, the mode of action of specific lipoproteins can now be deciphered. This information can prove important for the development of improved diagnostic tools and in the treatment of atherosclerosis.

Place, publisher, year, edition, pages
Nature Publishing Group, 2019
Keywords
Multidisciplinary Sciences
National Category
Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:mau:diva-4549 (URN)10.1038/s41598-019-43713-6 (DOI)000468281500021 ()31110185 (PubMedID)2-s2.0-85066021599 (Scopus ID)30138 (Local ID)30138 (Archive number)30138 (OAI)
Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2023-08-31Bibliographically approved
Falk, Y. Z., Engblom, J., Pedersen, J. S., Arnebrant, T. & Kocherbitov, V. (2018). Effects of Hydration on Structure and Phase Behavior of Pig Gastric Mucin Elucidated by SAXS (ed.). Journal of Physical Chemistry B, 122(30), 7539-7546
Open this publication in new window or tab >>Effects of Hydration on Structure and Phase Behavior of Pig Gastric Mucin Elucidated by SAXS
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2018 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 122, no 30, p. 7539-7546Article in journal (Refereed) Published
Abstract [en]

In this work small-angle X-ray scattering (SAXS) was used to study hydration and temperature-induced changes of pig gastric mucin (PGM) within the entire concentration range. The scattering is interpreted as originating from PGM fiber-like structures that adopt rod-like bottle-brush conformation in dilute solutions. On the basis of the knowledge about molecular structure of mucins and SAXS data for dilute solutions, we propose a theoretical model for predicting mucin conformation in solution and calculate the corresponding scattering profile. This bottle-brush model comprises a protein backbone with carbohydrate side chains and corresponding structural parameters, such as grafting distance and lengths of the backbone and side chains. It describes the experimental PGM data from dilute solutions in the full q range very well. It furthermore suggests that the carbohydrate side chains are grafted with a regular separation of around 5 nm and a length of 14 nm. The cross-section size with a radius of about 1 nm is also in accordance with the size of the carbohydrate units. Structuring of PGM solutions at higher concentrations was investigated by analyzing semidilute and concentrated PGM samples. Starting at about 20 wt %, Bragg peaks become clearly visible indicating a more ordered mucin system. In very dehydrated and fully dry mucin samples these peaks are not present indicating lack of long-range order. The SAXS data show that the structural change occurring at about 80 wt % mucin and 25 degrees C corresponds to a glass transition in agreement with our previous calorimetric results. Temperature also has an effect on the phase behavior of mucin. At intermediate levels of hydration, a phase transition is observed at about 60-70 degrees C. The main Bragg peak appears to split in two, indicating formation of a different structure at elevated temperatures. These findings are used to improve the PGM water phase diagram.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018
Keywords
Chemistry, Physical
National Category
Natural Sciences
Identifiers
urn:nbn:se:mau:diva-5260 (URN)10.1021/acs.jpcb.8b05496 (DOI)000440956300009 ()29989815 (PubMedID)2-s2.0-85049844913 (Scopus ID)26637 (Local ID)26637 (Archive number)26637 (OAI)
Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2024-02-05Bibliographically approved
Projects
Scattering in Confined and Sheared Geometries; Malmö University
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