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Balaz, Martina
Publications (10 of 19) Show all publications
Persson, M., Albet-Torres, N., Ionov, L., Sundberg, M., Höök, F., Diez, S., . . . Balaz, M. (2010). Heavy meromyosin molecules extending more than 50 nm above adsorbing electronegative surfaces.. Langmuir, 26(12), 9927-9936
Open this publication in new window or tab >>Heavy meromyosin molecules extending more than 50 nm above adsorbing electronegative surfaces.
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2010 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 26, no 12, p. 9927-9936Article in journal (Refereed) Published
Abstract [en]

In the in vitro motility assay, actin filaments are propelled by surface-adsorbed myosin motors, or rather, myosin motor fragments such as heavy meromyosin (HMM). Recently, efforts have been made to develop actomyosin powered nanodevices on the basis of this assay but such developments are hampered by limited understanding of the HMM adsorption geometry. Therefore, we here investigate the HMM adsorption geometries on trimethylchlorosilane- [TMCS-] derivatized hydrophobic surfaces and on hydrophilic negatively charged surfaces (SiO(2)). The TMCS surface is of great relevance in fundamental studies of actomyosin and both surface substrates are important for the development of motor powered nanodevices. Whereas both the TMCS and SiO(2) surfaces were nearly saturated with HMM (incubation at 120 microg mL(-1)) there was little actin binding on SiO(2) in the absence of ATP and no filament sliding in the presence of ATP. This contrasts with excellent actin-binding and motility on TMCS. Quartz crystal microbalance with dissipation (QCM-D) studies demonstrate a HMM layer with substantial protein mass up to 40 nm above the TMCS surface, considerably more than observed for myosin subfragment 1 (S1; 6 nm). Together with the excellent actin transportation on TMCS, this strongly suggests that HMM adsorbs to TMCS mainly via its most C-terminal tail part. Consistent with this idea, fluorescence interference contrast (FLIC) microscopy showed that actin filaments are held by HMM 38 +/- 2 nm above the TMCS-surface with the catalytic site, on average, 20-30 nm above the surface. Viewed in a context with FLIC, QCM-D and TIRF results, the lack of actin motility and the limited actin binding on SiO(2) shows that HMM adsorbs largely via the actin-binding region on this surface with the C-terminal coiled-coil tails extending >50 nm into solution. The results and new insights from this study are of value, not only for the development of motor powered nanodevices but also for the interpretation of fundamental biophysical studies of actomyosin function and for the understanding of surface-protein interactions in general.

National Category
Medical and Health Sciences
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-6446 (URN)10.1021/la100395a (DOI)20337414 (PubMedID)2-s2.0-77954603127 (Scopus ID)
Available from: 2010-06-22 Created: 2010-06-22 Last updated: 2017-12-12Bibliographically approved
Albet-Torres, N., Gunnarsson, A., Persson, M., Balaz, M., Höök, F. & Månsson, A. (2010). Molecular motors on lipid bilayers and silicon dioxide: different driving forces for adsorption. Soft Matter, 6(14), 3211-3219
Open this publication in new window or tab >>Molecular motors on lipid bilayers and silicon dioxide: different driving forces for adsorption
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2010 (English)In: Soft Matter, ISSN 1744-683X, E-ISSN 1744-6848, Vol. 6, no 14, p. 3211-3219Article in journal (Refereed) Published
Abstract [en]

Understanding how different types of interactions govern adsorption of the myosin motor fragment heavy meromyosin (HMM) onto different substrates is important in functional studies of actomyosin and for the development of motor powered lab-on-a-chip applications. In this study, we have combined in vitro motility assays and quartz crystal microbalance with dissipation (QCM-D) monitoring to investigate the underlying adsorption mechanisms of HMM onto supported lipid bilayers in comparison with pure and silanized SiO2. The QCM-D results, combined with data showing actin transportation by HMM adsorbed onto positively charged supported lipid bilayers, suggest reversible HMM surface adsorption via the negatively charged coiled-coil tail region. In contrast, the QCM-D data for HMM adsorption onto negatively charged lipids support a model according to which HMM adsorbs onto negatively charged surfaces largely via the positively charged actin binding regions. Adsorption studies at low (30-65 mM) and high (185-245 mM) ionic strengths onto piranha cleaned SiO2 surfaces (contact angle < 20 degrees) support this general model. However, unlike the situation for charged lipids, rinsing in high ionic strength solution caused only partial HMM desorption from SiO2, without restoration of actin propulsion by the remaining HMM molecules. This suggests that mechanisms other than electrostatic interactions are involved in the tethering of HMM heads to SiO2 surfaces. An expanded model for HMM adsorption is formulated on the basis of the data and the potential of the results for nanotechnological applications of actomyosin is discussed.

National Category
Natural Sciences
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-7222 (URN)10.1039/c0sm00019a (DOI)2-s2.0-77954610067 (Scopus ID)
Available from: 2010-08-13 Created: 2010-08-13 Last updated: 2017-12-12Bibliographically approved
Vikhorev, P., Vikhoreva, N., Sundberg, M., Balaz, M., Torres, N. A., Bunk, R., . . . Månsson, A. (2008). Diffusion dynamics of motor driven transport: gradient production and self-organization of surfaces.. Langmuir, 24(23), 13509-13517
Open this publication in new window or tab >>Diffusion dynamics of motor driven transport: gradient production and self-organization of surfaces.
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2008 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 24, no 23, p. 13509-13517Article in journal (Refereed) Published
Abstract [en]

The interaction between cytoskeletal filaments (e.g., actin filaments) and molecular motors (e.g., myosin) is the basis for many aspects of cell motility and organization of the cell interior. In the in vitro motility assay (IVMA), cytoskeletal filaments are observed while being propelled by molecular motors adsorbed to artificial surfaces (e.g., in studies of motor function). Here we integrate ideas that cytoskeletal filaments may be used as nanoscale templates in nanopatterning with a novel approach for the production of surface gradients of biomolecules and nanoscale topographical features. The production of such gradients is challenging but of increasing interest (e.g., in cell biology). First, we show that myosin-induced actin filament sliding in the IVMA can be approximately described as persistent random motion with a diffusion coefficient D) given by a relationship analogous to the Einstein equation (D = kT/gamma). In this relationship, the thermal energy (kT) and the drag coefficient (gamma) are substituted by a parameter related to the free-energy transduction by actomyosin and the actomyosin dissociation rate constant, respectively. We then demonstrate how the persistent random motion of actin filaments can be exploited in conceptually novel methods for the production of actin filament density gradients of predictable shapes. Because of regularly spaced binding sites (e.g., lysines and cysteines) the actin filaments act as suitable nanoscale scaffolds for other biomolecules (tested for fibronectin) or nanoparticles. This forms the basis for secondary chemical and topographical gradients with implications for cell biological studies and biosensing.

National Category
Natural Sciences
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-1858 (URN)10.1021/la8016112 (DOI)000261216500043 ()
Available from: 2010-04-06 Created: 2010-04-06 Last updated: 2017-12-12Bibliographically approved
Månsson, A., Balaz, M., Torres, N. A. & Rosengren, J. (2008). In vitro assays of molecular motors - impact of motor-surface interactions. Frontiers in Bioscience, 13(May 1), 5732-5754
Open this publication in new window or tab >>In vitro assays of molecular motors - impact of motor-surface interactions
2008 (English)In: Frontiers in Bioscience, ISSN 1093-9946, E-ISSN 1093-4715, Vol. 13, no May 1, p. 5732-5754Article, review/survey (Other academic) Published
Abstract [en]

In many types of biophysical studies of both single molecules and ensembles of molecular motors the motors are adsorbed to artificial surfaces. Some of the most important assay systems of this type (in vitro motility assays and related single molecule techniques) will be briefly described together with an account of breakthroughs in the understanding of actomyosin function that have resulted from their use. A poorly characterized, but potentially important, entity in these studies is the mechanism of motor adsorption to surfaces and the effects of motor surface interactions on experimental results. A better understanding of these phenomena is also important for the development of commercially viable nanotechnological applications powered by molecular motors. Here, we will consider several aspects of motor surface interactions with a particular focus on heavy meromyosin (HMM) from skeletal muscle. These aspects will be related to heavy meromyosin structure and relevant parts of the vast literature on protein-surface interactions for non-motor proteins. An overview of methods for studying motor-surface interactions will also be given. The information is used as a basis for further development of a model for HMM-surface interactions and is discussed in relation to experiments where nanopatterning has been employed for in vitro reconstruction of actomyosin order. The challenges and potentials of this approach in biophysical studies, compared to the use of self-assembly of biological components into supramolecular protein aggregates (e. g. myosin filaments) will be considered. Finally, this review will consider the implications for further developments of motor-powered lab-on-a-chip devices.

National Category
Organic Chemistry
Research subject
Natural Science, Biomedical Sciences; Natural Science, Organic Chemistry
Identifiers
urn:nbn:se:lnu:diva-5095 (URN)
Available from: 2010-04-28 Created: 2010-04-28 Last updated: 2017-12-12Bibliographically approved
Balaz, M., Sundberg, M., Persson, M., Kvassman, J.-O. & Månsson, A. (2007). "Effects of surface adsorption on catalytic activity of heavy meromyosin studied using fluorescent ATP analogue". Biochemistry, 24, 4917-4934
Open this publication in new window or tab >>"Effects of surface adsorption on catalytic activity of heavy meromyosin studied using fluorescent ATP analogue"
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2007 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 24, p. 4917-4934Article in journal (Refereed) Published
National Category
Natural Sciences
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-2360 (URN)
Available from: 2010-04-07 Created: 2010-04-07 Last updated: 2017-12-12Bibliographically approved
Torres, N. A., O'MAHONY, J., Charlton, C., Balaz, M., Lisboa, P., Aastrup, T., . . . Nicholls, I. A. (2007). Mode of Heavy Meromyosin Adsorption and Motor Function Correlated with Surface Hydrophobicity and Charge. Langmuir, 23, 11147-11156
Open this publication in new window or tab >>Mode of Heavy Meromyosin Adsorption and Motor Function Correlated with Surface Hydrophobicity and Charge
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2007 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 23, p. 11147-11156Article in journal (Refereed) Published
National Category
Natural Sciences
Research subject
Natural Science, Organic Chemistry; Biomedical Sciences, Pharmacology; Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-2341 (URN)
Available from: 2010-04-07 Created: 2010-04-07 Last updated: 2017-12-12Bibliographically approved
Sundberg, M., Balaz, M., Bunk, R., Rosengren-Holmberg, J., Montelius, L., Nicholls, I. A., . . . Månsson, A. (2006). Selective spatial localization of actomyosin motor function by chemical surface patterning. Langmuir, 22(17), 7302-7312
Open this publication in new window or tab >>Selective spatial localization of actomyosin motor function by chemical surface patterning
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2006 (English)In: Langmuir, Vol. 22, no 17, p. 7302-7312Article in journal (Refereed) Published
National Category
Natural Sciences
Research subject
Natural Science, Biomedical Sciences; Natural Science, Organic Chemistry; Biomedical Sciences, Pharmacology
Identifiers
urn:nbn:se:lnu:diva-689 (URN)
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2015-09-14Bibliographically approved
Månsson, A., Sundberg, M., Bunk, R., Balaz, M., Nicholls, I. A., Omling, P., . . . Montelius, L. (2005). Actin-based molecular motors for cargo transportation in nanotechnology - Potentials and challenges. IEEE transactions on advanced packaging, 28 (4), 547-555
Open this publication in new window or tab >>Actin-based molecular motors for cargo transportation in nanotechnology - Potentials and challenges
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2005 (English)In: IEEE transactions on advanced packaging, Vol. 28 (4), p. 547-555Article in journal (Refereed) Published
Research subject
Natural Science, Biomedical Sciences; Natural Science, Organic Chemistry; Biomedical Sciences, Pharmacology
Identifiers
urn:nbn:se:lnu:diva-686 (URN)
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2015-09-14Bibliographically approved
Balaz, M. & Månsson, A. (2005). Detection of small differences in actomyosin function using actin labeled with different phalloidin conjugates. Analytical biochemistry, 338 (2), 224-236
Open this publication in new window or tab >>Detection of small differences in actomyosin function using actin labeled with different phalloidin conjugates
2005 (English)In: Analytical biochemistry, Vol. 338 (2), p. 224-236Article in journal (Refereed) Published
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-674 (URN)
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2015-09-14Bibliographically approved
Balaz, M. & Månsson, A. (2005). Simultaneous studies of different actins in the in vitro motility assay. Biophysical journal, 88 (1), 503A-503A
Open this publication in new window or tab >>Simultaneous studies of different actins in the in vitro motility assay
2005 (English)In: Biophysical journal, Vol. 88 (1), p. 503A-503AArticle in journal (Refereed) Published
Research subject
Natural Science, Biomedical Sciences
Identifiers
urn:nbn:se:lnu:diva-675 (URN)
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2015-09-14Bibliographically approved
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