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Elinder, Fredrik, ProfessorORCID iD iconorcid.org/0000-0001-9125-5583
Alternative names
Publications (10 of 59) Show all publications
Wang, K., Nilsson, M., Angelini, M., Olcese, R., Elinder, F. & Pantazis, A. (2025). A rich conformational palette underlies human CaV2.1-channel availability. Nature Communications, 16(1), Article ID 3815.
Open this publication in new window or tab >>A rich conformational palette underlies human CaV2.1-channel availability
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2025 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 16, no 1, article id 3815Article in journal (Refereed) Published
Abstract [en]

Depolarization-evoked opening of CaV2.1 (P/Q-type) Ca2+-channels triggers neurotransmitter release, while voltage-dependent inactivation (VDI) limits channel availability to open, contributing to synaptic plasticity. The mechanism of CaV2.1 response to voltage is unclear. Using voltage-clamp fluorometry and kinetic modeling, we optically track and physically characterize the structural dynamics of the four CaV2.1 voltage-sensor domains (VSDs). The VSDs are differentially sensitive to voltage changes, both brief and long-lived. VSD-I seems to directly drive opening and convert between two modes of function, associated with VDI. VSD-II is apparently voltage-insensitive. VSD-III and VSD-IV sense more negative voltages and undergo voltage-dependent conversion uncorrelated with VDI. Auxiliary β-subunits regulate VSD-I-to-pore coupling and VSD conversion kinetics. Hence, the central role of CaV2.1 channels in synaptic release, and their contribution to plasticity, memory formation and learning, can arise from the voltage-dependent conformational changes of VSD-I.

Place, publisher, year, edition, pages
Springer Nature, 2025
National Category
Neurosciences
Identifiers
urn:nbn:se:liu:diva-213255 (URN)10.1038/s41467-025-58884-2 (DOI)001473866400029 ()40268901 (PubMedID)2-s2.0-105003414058 (Scopus ID)
Funder
Knut and Alice Wallenberg Foundation, NASwedish Research Council, 2022-00574Swedish Research Council, 2019-00988Swedish Research Council, 2020-01019The Swedish Brain Foundation, 2022-0219The Swedish Brain Foundation, 2022-0003The Swedish Brain Foundation, 2023-0025Swedish Heart Lung Foundation, 20210596
Note

Funding Agencies|Lions Forskningsfond mot Folksjukdomar Ph.D. support; NIH/NIGMS [R35GM131896]; Start-up funds from the Linkoeping University Wallenberg Center for Molecular Medicine / the Knut and Alice Wallenberg Foundation; Hjaernfonden (The Swedish Brain Foundation) grants [FO2022-0219, FO2022-0003, FO2023-0025]; Hjaert-Lung Fonden (The Swedish Heart-Lung Foundation) [20210596]; Vetenskapsradet (The Swedish Research Council) grants [2020-01019, 2019-00988, 2022-00574]

Available from: 2025-04-25 Created: 2025-04-25 Last updated: 2025-05-24
Silverå Ejneby, M., Wallner, B. & Elinder, F. (2020). Coupling stabilizers open KV1-type potassium channels. Proceedings of the National Academy of Sciences of the United States of America, 117(43), 27016-27021
Open this publication in new window or tab >>Coupling stabilizers open KV1-type potassium channels
2020 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 117, no 43, p. 27016-27021Article in journal (Refereed) Published
Abstract [en]

The opening and closing of voltage-gated ion channels are regulated by voltage sensors coupled to a gate that controls the ion flux across the cellular membrane. Modulation of any part of gating constitutes an entry point for pharmacologically regulating channel function. Here, we report on the discovery of a large family of warfarin-like compounds that open the two voltage-gated type 1 potassium (KV1) channels KV1.5 and Shaker, but not the related KV2-, KV4-, or KV7-type channels. These negatively charged compounds bind in the open state to positively charged arginines and lysines between the intracellular ends of the voltage-sensor domains and the pore domain. This mechanism of action resembles that of endogenous channel-opening lipids and opens up an avenue for the development of ion-channel modulators.

Place, publisher, year, edition, pages
Washington, DC, United States: The National Academy of Sciences, 2020
Keywords
Kv1 channel, VSD-to-pore coupling, potassium-channel openers
National Category
Biochemistry Molecular Biology
Identifiers
urn:nbn:se:liu:diva-171109 (URN)10.1073/pnas.2007965117 (DOI)000582743300060 ()33051293 (PubMedID)2-s2.0-85094813055 (Scopus ID)
Funder
Swedish Research Council, 2016- 02615Swedish Heart Lung Foundation, 20150672The Swedish Brain Foundation, 2016-0326
Note

Funding agencies: Swedish Research CouncilSwedish Research Council [2016-02615]; Swedish Heart-Lung FoundationSwedish Heart-Lung Foundation [20150672]; Swedish Brain Foundation [2016-0326]

Available from: 2020-11-05 Created: 2020-11-05 Last updated: 2025-02-20Bibliographically approved
Wickström, W., Spreco, A., Bargoria, V., Elinder, F., Hansson, P.-O., Dahlström, Ö. & Timpka, T. (2019). Perceptions of Overuse Injury Among Swedish Ultramarathon and Marathon Runners: Cross-Sectional Study Based on the Illness Perception Questionnaire Revised (IPQ-R). Frontiers in Psychology, 10, 1-11, Article ID 2406.
Open this publication in new window or tab >>Perceptions of Overuse Injury Among Swedish Ultramarathon and Marathon Runners: Cross-Sectional Study Based on the Illness Perception Questionnaire Revised (IPQ-R)
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2019 (English)In: Frontiers in Psychology, E-ISSN 1664-1078, Vol. 10, p. 1-11, article id 2406Article in journal (Refereed) Published
Abstract [en]

Background: Long-distance runners’ understandings of overuse injuries are not well known which decreases the possibilities for prevention. The common sense model (CSM) outlines that runners’ perceptions of a health problem can be described using the categories identity, consequence, timeline, personal control, and cause. The aim of this study was to use the CSM to investigate perceptions of overuse injury among long-distance runners with different exercise loads.

Methods: The study used a cross-sectional design. An adapted version of the illness perception questionnaire revised (IPQ-R) derived from the CSM was used to investigate Swedish ultramarathon and marathon runners’ perceptions of overuse injuries. Cluster analysis was employed for categorizing runners into high and low exercise load categories. A Principal Component Analysis was thereafter used to group variables describing injury causes. Multiple logistic regression methods were finally applied using high exercise load as endpoint variable and CSM items representing perceptions of injury identity, consequence, timeline, personal control, and causes as explanatory variables.

Results: Complete data sets were collected from 165/443 (37.2%) runners. The symptoms most commonly associated with overuse injury were pain (80.1% of the runners), stiff muscles (54.1%), and stiff joints (42.0%). Overuse injury was perceived to be characterized by the possibility of personal control (stated by 78.7% of the runners), treatability (70.4%), and that the injury context was comprehensible (69.3%). The main injury causes highlighted were runner biomechanics (stated by 78.3%), the runner’s personality (72.4%), and running surface biomechanics (70.0%). Among men, a belief in that personality contributes to overuse injury increased the likelihood of belonging to the high exercise load category [Odds ratio (OR) 2.10 (95% Confidence interval (95% CI) 1.38–3.19); P = 0.001], while beliefs in that running biomechanics [OR 0.56 (95% CI 0.37–0.85); P = 0.006) and mileage (OR 0.72 (95% CI 0.54–0.96); P = 0.026] causes injury decreased the likelihood. In women, a strong perception that overuse injuries can be controlled by medical interventions decreased the likelihood of high exercise load [OR 0.68 (95% CI 0.52–0.89); P = 0.005].

Conclusion: This study indicates that recognition among long-distance runners of the association between own decisions in overuse injury causation is accentuated by increased exercise loads.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2019
Keywords
Illness perceptions, long-distance running, overuse injury, exercise load, common sense model of illness, sports psychology
National Category
Public Health, Global Health and Social Medicine Sport and Fitness Sciences Physiotherapy
Identifiers
urn:nbn:se:liu:diva-161230 (URN)10.3389/fpsyg.2019.02406 (DOI)000494658900001 ()
Note

Funding agencies: Swedish Centre for Sports Research (CIF) [P2018-0194]

Available from: 2019-10-24 Created: 2019-10-24 Last updated: 2025-02-20
Silverå Ejneby, M., Wu, X., Ottosson, N., Münger, E. P., Lundström, I., Konradsson, P. & Elinder, F. (2018). Atom-by-atom tuning of the electrostatic potassium-channel modulator dehydroabietic acid. The Journal of General Physiology, 150(5), 731-750
Open this publication in new window or tab >>Atom-by-atom tuning of the electrostatic potassium-channel modulator dehydroabietic acid
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2018 (English)In: The Journal of General Physiology, ISSN 0022-1295, E-ISSN 1540-7748, Vol. 150, no 5, p. 731-750Article in journal (Refereed) Published
Abstract [en]

Dehydroabietic acid (DHAA) is a naturally occurring component of pine resin that was recently shown to open voltage-gated potassium (KV) channels. The hydrophobic part of DHAA anchors the compound near the channel’s positively charged voltage sensor in a pocket between the channel and the lipid membrane. The negatively charged carboxyl group exerts an electrostatic effect on the channel’s voltage sensor, leading to the channel opening. In this study, we show that the channel-opening effect increases as the length of the carboxyl-group stalk is extended until a critical length of three atoms is reached. Longer stalks render the compounds noneffective. This critical distance is consistent with a simple electrostatic model in which the charge location depends on the stalk length. By combining an effective anchor with the optimal stalk length, we create a compound that opens the human KV7.2/7.3 (M type) potassium channel at a concentration of 1 µM. These results suggest that a stalk between the anchor and the effector group is a powerful way of increasing the potency of a channel-opening drug.

Place, publisher, year, edition, pages
New York, United States: Rockefeller Institute for Medical Research, 2018
National Category
Physiology and Anatomy
Identifiers
urn:nbn:se:liu:diva-147837 (URN)10.1085/jgp.201711965 (DOI)000434417800008 ()2-s2.0-85046705149 (Scopus ID)
Note

Funding agencies: Swedish Research Council [2016-02615]; Swedish Heart-Lung Foundation [20150672]; Swedish Brain Foundation [2016-0326]

Available from: 2018-05-15 Created: 2018-05-15 Last updated: 2025-02-10Bibliographically approved
Salari, S., Silverå Ejneby, M., Brask, J. & Elinder, F. (2018). Isopimaric acid - a multi-targeting ion channel modulator reducing excitability and arrhythmicity in a spontaneously beating mouse atrial cell line. Acta Physiologica, 222(1), Article ID e12895.
Open this publication in new window or tab >>Isopimaric acid - a multi-targeting ion channel modulator reducing excitability and arrhythmicity in a spontaneously beating mouse atrial cell line
2018 (English)In: Acta Physiologica, ISSN 1748-1708, E-ISSN 1748-1716, Vol. 222, no 1, article id e12895Article in journal (Refereed) Published
Abstract [en]

AimAtrial fibrillation is the most common persistent cardiac arrhythmia, and it is not well controlled by present drugs. Because some resin acids open voltage-gated potassium channels and reduce neuronal excitability, we explored the effects of the resin acid isopimaric acid (IPA) on action potentials and ion currents in cardiomyocytes. MethodsSpontaneously beating mouse atrial HL-1 cells were investigated with the whole-cell patch-clamp technique. Results1-25 mol L-1 IPA reduced the action potential frequency by up to 50%. The effect of IPA on six different voltage-gated ion channels was investigated; most voltage-dependent parameters of ion channel gating were shifted in the negative direction along the voltage axis, consistent with a hypothesis that a lipophilic and negatively charged compound binds to the lipid membrane close to the positively charged voltage sensor of the ion channels. The major finding was that IPA inactivated sodium channels and L- and T-type calcium channels and activated the rapidly activating potassium channel and the transient outward potassium channel. Computer simulations of IPA effects on all of the ion currents were consistent with a reduced excitability, and they also showed that effects on the Na channel played the largest role to reduce the action potential frequency. Finally, induced arrhythmia in the HL-1 cells was reversed by IPA. ConclusionLow concentrations of IPA reduced the action potential frequency and restored regular firing by altering the voltage dependencies of several voltage-gated ion channels. These findings can form the basis for a new pharmacological strategy to treat atrial fibrillation.

Place, publisher, year, edition, pages
Wiley-VCH Verlagsgesellschaft, 2018
Keywords
arrhythmia; atrial fibrillation; ion channels; isopimaric acid; patch clamp; resin acid
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:liu:diva-144564 (URN)10.1111/apha.12895 (DOI)000419864000009 ()28514017 (PubMedID)
Note

Funding Agencies|Swedish Research Council; Swedish Heart-Lung Foundation; Swedish Brain Foundation; ALF

Available from: 2018-01-29 Created: 2018-01-29 Last updated: 2024-01-10
Elinder, F. & Börjesson, S. I. (2017). Actions and Mechanisms of Polyunsaturated Fatty Acids on Voltage-Gated Ion Channels. Frontiers in Physiology, 8, Article ID 43.
Open this publication in new window or tab >>Actions and Mechanisms of Polyunsaturated Fatty Acids on Voltage-Gated Ion Channels
2017 (English)In: Frontiers in Physiology, E-ISSN 1664-042X, Vol. 8, article id 43Article, review/survey (Refereed) Published
Abstract [en]

Polyunsaturated fatty acids (PUFAs) act on most ion channels, thereby having significant physiological and pharmacological effects. In this review we summarize data from numerous PUFAs on voltage-gated ion channels containing one or several voltage-sensor domains, such as voltage-gated sodium (NaV), potassium (KV), calcium (CaV), and proton (HV) channels, as well as calcium-activated potassium (KCa), and transient receptor potential (TRP) channels. Some effects of fatty acids appear to be channel specific, whereas others seem to be more general. Common features for the fatty acids to act on the ion channels are at least two double bonds in cis geometry and a charged carboxyl group. In total we identify and label five different sites for the PUFAs. PUFA site 1: The intracellular cavity. Binding of PUFA reduces the current, sometimes as a time-dependent block, inducing an apparent inactivation. PUFA site 2: The extracellular entrance to the pore. Binding leads to a block of the channel. PUFA site 3: The intracellular gate. Binding to this site can bend the gate open and increase the current. PUFA site 4: The interface between the extracellular leaflet of the lipid bilayer and the voltage-sensor domain. Binding to this site leads to an opening of the channel via an electrostatic attraction between the negatively charged PUFA and the positively charged voltage sensor. PUFA site 5: The interface between the extracellular leaflet of the lipid bilayer and the pore domain. Binding to this site affects slow inactivation. This mapping of functional PUFA sites can form the basis for physiological and pharmacological modifications of voltage-gated ion channels.

Place, publisher, year, edition, pages
FRONTIERS MEDIA SA, 2017
Keywords
voltage-gated ion channels; polyunsaturated fatty acids; voltage sensor domain; S4; Excitability disorders
National Category
Biochemistry Molecular Biology
Identifiers
urn:nbn:se:liu:diva-134980 (URN)10.3389/fphys.2017.00043 (DOI)000393235000001 ()28220076 (PubMedID)
Note

Funding Agencies|Swedish Research Council; Swedish Brain Foundation; Swedish Society for Medical Research; Swedish Heart-Lung Foundation

Available from: 2017-03-06 Created: 2017-03-06 Last updated: 2025-02-20
Lundengård, K., Cedersund, G., Sten, S., Leong, F., Smedberg, A., Elinder, F. & Engström, M. (2016). Mechanistic Mathematical Modeling Tests Hypotheses of the Neurovascular Coupling in fMRI. PloS Computational Biology, 12(6), Article ID e1004971.
Open this publication in new window or tab >>Mechanistic Mathematical Modeling Tests Hypotheses of the Neurovascular Coupling in fMRI
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2016 (English)In: PloS Computational Biology, ISSN 1553-734X, E-ISSN 1553-7358, Vol. 12, no 6, article id e1004971Article in journal (Refereed) Published
Abstract [en]

Functional magnetic resonance imaging (fMRI) measures brain activity by detecting the blood-oxygen-level dependent (BOLD) response to neural activity. The BOLD response depends on the neurovascular coupling, which connects cerebral blood flow, cerebral blood volume, and deoxyhemoglobin level to neuronal activity. The exact mechanisms behind this neurovascular coupling are not yet fully investigated. There are at least three different ways in which these mechanisms are being discussed. Firstly, mathematical models involving the so-called Balloon model describes the relation between oxygen metabolism, cerebral blood volume, and cerebral blood flow. However, the Balloon model does not describe cellular and biochemical mechanisms. Secondly, the metabolic feedback hypothesis, which is based on experimental findings on metabolism associated with brain activation, and thirdly, the neurotransmitter feed-forward hypothesis which describes intracellular pathways leading to vasoactive substance release. Both the metabolic feedback and the neurotransmitter feed-forward hypotheses have been extensively studied, but only experimentally. These two hypotheses have never been implemented as mathematical models. Here we investigate these two hypotheses by mechanistic mathematical modeling using a systems biology approach; these methods have been used in biological research for many years but never been applied to the BOLD response in fMRI. In the current work, model structures describing the metabolic feedback and the neurotransmitter feed-forward hypotheses were applied to measured BOLD responses in the visual cortex of 12 healthy volunteers. Evaluating each hypothesis separately shows that neither hypothesis alone can describe the data in a biologically plausible way. However, by adding metabolism to the neurotransmitter feed-forward model structure, we obtained a new model structure which is able to fit the estimation data and successfully predict new, independent validation data. These results open the door to a new type of fMRI analysis that more accurately reflects the true neuronal activity.

Place, publisher, year, edition, pages
PUBLIC LIBRARY SCIENCE, 2016
National Category
Bioinformatics (Computational Biology)
Identifiers
urn:nbn:se:liu:diva-130437 (URN)10.1371/journal.pcbi.1004971 (DOI)000379349700045 ()27310017 (PubMedID)
Note

Funding Agencies|Swedish Research council [2014-6249]; Knut and Alice Wallenbergs foundation, KAW [2013.0076]; Research council of Southeast Sweden [FORSS-481691]; Linkoping University

Available from: 2016-08-06 Created: 2016-08-05 Last updated: 2020-08-14
Conti, L., Renhorn, J., Gabrielsson, A., Turesson, F., Liin, S., Lindahl, E. & Elinder, F. (2016). Reciprocal voltage sensor-to-pore coupling leads to potassium channel C-type inactivation. Scientific Reports, 6, Article ID 27562.
Open this publication in new window or tab >>Reciprocal voltage sensor-to-pore coupling leads to potassium channel C-type inactivation
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2016 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 6, article id 27562Article in journal (Refereed) Published
Abstract [en]

Voltage-gated potassium channels open at depolarized membrane voltages. A prolonged depolarization causes a rearrangement of the selectivity filter which terminates the conduction of ions - a process called slow or C-type inactivation. How structural rearrangements in the voltage-sensor domain (VSD) cause alteration in the selectivity filter, and vice versa, are not fully understood. We show that pulling the pore domain of the Shaker potassium channel towards the VSD by a Cd2+ bridge accelerates C-type inactivation. Molecular dynamics simulations show that such pulling widens the selectivity filter and disrupts the K+ coordination, a hallmark for C-type inactivation. An engineered Cd2+ bridge within the VSD also affect C-type inactivation. Conversely, a pore domain mutation affects VSD gating-charge movement. Finally, C-type inactivation is caused by the concerted action of distant amino acid residues in the pore domain. All together, these data suggest a reciprocal communication between the pore domain and the VSD in the extracellular portion of the channel.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP, 2016
National Category
Structural Biology
Identifiers
urn:nbn:se:liu:diva-130064 (URN)10.1038/srep27562 (DOI)000377343800001 ()27278891 (PubMedID)
Note

Funding Agencies|Swedish Research Council; Swedish Brain Foundation; Swedish Heart-Lung Foundation; Swedish e-Science Research Center; Foundation Blanceflor Boncompagni Ludovisi, nee Bildt

Available from: 2016-07-06 Created: 2016-07-06 Last updated: 2022-09-15
Yazdi, S., Stein, M., Elinder, F., Andersson, M. & Lindahl, E. (2016). The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel. PloS Computational Biology, 12(1), e1004704
Open this publication in new window or tab >>The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel
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2016 (English)In: PloS Computational Biology, ISSN 1553-734X, E-ISSN 1553-7358, Vol. 12, no 1, p. e1004704-Article in journal (Refereed) Published
Abstract [en]

Voltage-gated potassium (K-V) channels are membrane proteins that respond to changes in membrane potential by enabling K+ ion flux across the membrane. Polyunsaturated fatty acids (PUFAs) induce channel opening by modulating the voltage-sensitivity, which can provide effective treatment against refractory epilepsy by means of a ketogenic diet. While PUFAs have been reported to influence the gating mechanism by electrostatic interactions to the voltage-sensor domain (VSD), the exact PUFA-protein interactions are still elusive. In this study, we report on the interactions between the Shaker K-V channel in open and closed states and a PUFA-enriched lipid bilayer using microsecond molecular dynamics simulations. We determined a putative PUFA binding site in the open state of the channel located at the protein-lipid interface in the vicinity of the extracellular halves of the S3 and S4 helices of the VSD. In particular, the lipophilic PUFA tail covered a wide range of non-specific hydrophobic interactions in the hydrophobic central core of the protein-lipid interface, while the carboxylic head group displayed more specific interactions to polar/charged residues at the extracellular regions of the S3 and S4 helices, encompassing the S3-S4 linker. Moreover, by studying the interactions between saturated fatty acids (SFA) and the Shaker K-V channel, our study confirmed an increased conformational flexibility in the polyunsaturated carbon tails compared to saturated carbon chains, which may explain the specificity of PUFA action on channel proteins.

Place, publisher, year, edition, pages
PUBLIC LIBRARY SCIENCE, 2016
National Category
Clinical Medicine
Identifiers
urn:nbn:se:liu:diva-125693 (URN)10.1371/journal.pcbi.1004704 (DOI)000369366100033 ()26751683 (PubMedID)
Note

Funding Agencies|Max Planck Society for Advancement of Science; Excellence Initiative "Research Center for Dynamic Systems: Biosystems Engineering"; Swedish Research Council [2013-5901]; Swedish Heart-Lung Foundation; Swedish Brain Foundation; Marie Curie Career Integration Grant [FP7-MC-CIG-618558]; Magnus Bergvalls Stiftelse [2014-00170]; Angstromke Wibergs Stiftelse [M14-0245]; Swedish e-Science Research Center (SeRC)

Available from: 2016-03-01 Created: 2016-02-29 Last updated: 2018-01-25
Johansson, P., Jullesson, D., Elfwing, A., Liin, S., Musumeci, C., Zeglio, E., . . . Inganäs, O. (2015). Electronic polymers in lipid membranes. Scientific Reports, 5(11242)
Open this publication in new window or tab >>Electronic polymers in lipid membranes
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2015 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 5, no 11242Article in journal (Refereed) Published
Abstract [en]

Electrical interfaces between biological cells and man-made electrical devices exist in many forms, but it remains a challenge to bridge the different mechanical and chemical environments of electronic conductors (metals, semiconductors) and biosystems. Here we demonstrate soft electrical interfaces, by integrating the metallic polymer PEDOT-S into lipid membranes. By preparing complexes between alkyl-ammonium salts and PEDOT-S we were able to integrate PEDOT-S into both liposomes and in lipid bilayers on solid surfaces. This is a step towards efficient electronic conduction within lipid membranes. We also demonstrate that the PEDOT-S@alkyl-ammonium: lipid hybrid structures created in this work affect ion channels in the membrane of Xenopus oocytes, which shows the possibility to access and control cell membrane structures with conductive polyelectrolytes.

Place, publisher, year, edition, pages
Nature Publishing Group, 2015
National Category
Biophysics
Identifiers
urn:nbn:se:liu:diva-120045 (URN)10.1038/srep11242 (DOI)000356090400002 ()26059023 (PubMedID)
Note

Funding Agencies|Knut and Alice Wallenberg Foundation; Swedish Research Council

Available from: 2015-07-06 Created: 2015-07-06 Last updated: 2025-02-20
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ORCID iD: ORCID iD iconorcid.org/0000-0001-9125-5583

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