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Correa, Y., Ravel, M., Imbert, M., Waldie, S., Clifton, L., Terry, A., . . . Del Giudice, R. (2024). Lipid exchange of apolipoprotein A-I amyloidogenic variants in reconstituted high-density lipoprotein with artificial membranes. Protein Science, 33(5), Article ID e4987.
Open this publication in new window or tab >>Lipid exchange of apolipoprotein A-I amyloidogenic variants in reconstituted high-density lipoprotein with artificial membranes
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2024 (English)In: Protein Science, ISSN 0961-8368, E-ISSN 1469-896X, Vol. 33, no 5, article id e4987Article in journal (Refereed) Published
Abstract [en]

High-density lipoproteins (HDLs) are responsible for removing cholesterol from arterial walls, through a process known as reverse cholesterol transport. The main protein in HDL, apolipoprotein A-I (ApoA-I), is essential to this process, and changes in its sequence significantly alter HDL structure and functions. ApoA-I amyloidogenic variants, associated with a particular hereditary degenerative disease, are particularly effective at facilitating cholesterol removal, thus protecting carriers from cardiovascular disease. Thus, it is conceivable that reconstituted HDL (rHDL) formulations containing ApoA-I proteins with functional/structural features similar to those of amyloidogenic variants hold potential as a promising therapeutic approach. Here we explored the effect of protein cargo and lipid composition on the function of rHDL containing one of the ApoA-I amyloidogenic variants G26R or L174S by Fourier transformed infrared spectroscopy and neutron reflectometry. Moreover, small-angle x-ray scattering uncovered the structural and functional differences between rHDL particles, which could help to comprehend higher cholesterol efflux activity and apparent lower phospholipid (PL) affinity. Our findings indicate distinct trends in lipid exchange (removal vs. deposition) capacities of various rHDL particles, with the rHDL containing the ApoA-I amyloidogenic variants showing a markedly lower ability to remove lipids from artificial membranes compared to the rHDL containing the native protein. This effect strongly depends on the level of PL unsaturation and on the particles' ultrastructure. The study highlights the importance of the protein cargo, along with lipid composition, in shaping rHDL structure, contributing to our understanding of lipid-protein interactions and their behavior.

Place, publisher, year, edition, pages
John Wiley & Sons, 2024
Keywords
amyloidogenic variants, apolipoprotein A-I, high-density lipoprotein, reconstituted HDL
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:mau:diva-66837 (URN)10.1002/pro.4987 (DOI)001201388600001 ()38607188 (PubMedID)2-s2.0-85190272905 (Scopus ID)
Available from: 2024-04-22 Created: 2024-04-22 Last updated: 2024-05-20Bibliographically approved
Wolff, M., Frielinghaus, H., Cárdenas, M., Gonzalez, J. F., Theis-Bröhl, K., Softwedel, O., . . . Gutfreund, P. (2023). Grazing incidence neutron scattering for the study of solid–liquid interfaces. In: Reference Module in Chemistry, Molecular Sciences and Chemical Engineering: . Elsevier
Open this publication in new window or tab >>Grazing incidence neutron scattering for the study of solid–liquid interfaces
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2023 (English)In: Reference Module in Chemistry, Molecular Sciences and Chemical Engineering, Elsevier, 2023Chapter in book (Refereed)
Abstract [en]

Neutrons are characterized by a low absorption in many engineering materials. At the same time the scattering cross section of light elements, such as hydrogen and deuterium, may be large. These properties make neutron scattering experiments performed under grazing incidence geometry an excellent tool for the study of solid–liquid interfaces. In this review we describe the basic concepts of neutron reflection and grazing incidence scattering experiments as well as experimental procedures and sample cells. The full power of the method is exemplified on a range of science areas, including polymers, bio- and ionic liquid lubricants, electrolytes as well as bio-membranes or magnetic liquids.

Place, publisher, year, edition, pages
Elsevier, 2023
Keywords
Grazing incidence scattering, Neutron reflectometry, Solid–liquid interface
National Category
Chemical Engineering
Identifiers
urn:nbn:se:mau:diva-56106 (URN)10.1016/b978-0-323-85669-0.00014-3 (DOI)
Note

encyclopedia entry 

Available from: 2022-11-17 Created: 2022-11-17 Last updated: 2022-11-17Bibliographically approved
Correa, Y., Del Giudice, R., Waldie, S., Thépaut, M., Micciula, S., Gerelli, Y., . . . Cárdenas, M. (2023). High-Density Lipoprotein function is modulated by the SARS-CoV-2 spike protein in a lipid-type dependent manner.. Journal of Colloid and Interface Science, 645, 627-638, Article ID S0021-9797(23)00736-1.
Open this publication in new window or tab >>High-Density Lipoprotein function is modulated by the SARS-CoV-2 spike protein in a lipid-type dependent manner.
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2023 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 645, p. 627-638, article id S0021-9797(23)00736-1Article in journal (Refereed) Published
Abstract [en]

There is a close relationship between the SARS-CoV-2 virus and lipoproteins, in particular high-density lipoprotein (HDL). The severity of the coronavirus disease 2019 (COVID-19) is inversely correlated with HDL plasma levels. It is known that the SARS-CoV-2 spike (S) protein binds the HDL particle, probably depleting it of lipids and altering HDL function. Based on neutron reflectometry (NR) and the ability of HDL to efflux cholesterol from macrophages, we confirm these observations and further identify the preference of the S protein for specific lipids and the consequent effects on HDL function on lipid exchange ability. Moreover, the effect of the S protein on HDL function differs depending on the individuals lipid serum profile. Contrasting trends were observed for individuals presenting low triglycerides/high cholesterol serum levels (LTHC) compared to high triglycerides/high cholesterol (HTHC) or low triglycerides/low cholesterol serum levels (LTLC). Collectively, these results suggest that the S protein interacts with the HDL particle and, depending on the lipid profile of the infected individual, it impairs its function during COVID-19 infection, causing an imbalance in lipid metabolism.

Place, publisher, year, edition, pages
Elsevier, 2023
Keywords
COVID-19, Cholesterol efflux capacity, Deuterated cholesterol, HDL, Lipid metabolism, Lipids, Neutron reflection, SARS-CoV-2 spike protein
National Category
Medicinal Chemistry
Identifiers
urn:nbn:se:mau:diva-61402 (URN)10.1016/j.jcis.2023.04.137 (DOI)001004237100001 ()37167912 (PubMedID)2-s2.0-85158888783 (Scopus ID)
Available from: 2023-06-26 Created: 2023-06-26 Last updated: 2024-04-04Bibliographically approved
Cárdenas, M., Campbell, R. A., Arteta, M. Y., Lawrence, M. J. & Sebastiani, F. (2023). Review of structural design guiding the development of lipid nanoparticles for nucleic acid delivery. Current Opinion in Colloid & Interface Science, 66, Article ID 101705.
Open this publication in new window or tab >>Review of structural design guiding the development of lipid nanoparticles for nucleic acid delivery
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2023 (English)In: Current Opinion in Colloid & Interface Science, ISSN 1359-0294, E-ISSN 1879-0399, Vol. 66, article id 101705Article, review/survey (Refereed) Published
Abstract [en]

Lipid nanoparticles (LNPs) are the most versatile and successful gene delivery systems, notably highlighted by their use in vaccines against COVID-19. LNPs have a well-defined core-shell structure, each region with its own distinctive compositions, suited for a wide range of in vivo delivery applications. Here, we discuss how a detailed knowledge of LNP structure can guide LNP formulation to improve the efficiency of delivery of their nucleic acid payload. Perspectives are detailed on how LNP structural design can guide more efficient nucleic acid transfection. Views on key physical characterization techniques needed for such developments are outlined including opinions on biophysical approaches both correlating structure with functionality in biological fluids and improving their ability to escape the endosome and deliver they payload.

Place, publisher, year, edition, pages
Elsevier, 2023
Keywords
Lipid nanoparticles, Nucleic acid delicery, Structure-function, Cationic
National Category
Biophysics
Identifiers
urn:nbn:se:mau:diva-61924 (URN)10.1016/j.cocis.2023.101705 (DOI)001025798000001 ()2-s2.0-85162178818 (Scopus ID)
Available from: 2023-08-16 Created: 2023-08-16 Last updated: 2023-08-16Bibliographically approved
Paracini, N., Gutfreund, P., Welbourn, R., Gonzalez-Martinez, J. F., Zhu, K., Miao, Y., . . . Cárdenas, M. (2023). Structural Characterization of Nanoparticle-Supported Lipid Bilayer Arrays by Grazing Incidence X-ray and Neutron Scattering. ACS Applied Materials and Interfaces, 15(3), 3772-3780
Open this publication in new window or tab >>Structural Characterization of Nanoparticle-Supported Lipid Bilayer Arrays by Grazing Incidence X-ray and Neutron Scattering
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2023 (English)In: ACS Applied Materials and Interfaces, ISSN 1944-8244, E-ISSN 1944-8252, Vol. 15, no 3, p. 3772-3780Article in journal (Refereed) Published
Abstract [en]

Arrays of nanoparticle-supported lipid bilayers (nanoSLB) are lipid-coated nanopatterned interfaces that provide a platform to study curved model biological membranes using surface-sensitive techniques. We combined scattering techniques with direct imaging, to gain access to sub-nanometer scale structural information on stable nanoparticle monolayers assembled on silicon crystals in a noncovalent manner using a Langmuir-Schaefer deposition. The structure of supported lipid bilayers formed on the nanoparticle arrays via vesicle fusion was investigated using a combination of grazing incidence X-ray and neutron scattering techniques complemented by fluorescence microscopy imaging. Ordered nanoparticle assemblies were shown to be suitable and stable substrates for the formation of curved and fluid lipid bilayers that retained lateral mobility, as shown by fluorescence recovery after photobleaching and quartz crystal microbalance measurements. Neutron reflectometry revealed the formation of high-coverage lipid bilayers around the spherical particles together with a flat lipid bilayer on the substrate below the nanoparticles. The presence of coexisting flat and curved supported lipid bilayers on the same substrate, combined with the sub-nanometer accuracy and isotopic sensitivity of grazing incidence neutron scattering, provides a promising novel approach to investigate curvature-dependent membrane phenomena on supported lipid bilayers.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2023
Keywords
GISANS, GISAXS, membrane curvature, model membranes, nanoparticle-supported lipid bilayers, nanoSLB, neutron reflectometry
National Category
Chemical Sciences
Identifiers
urn:nbn:se:mau:diva-58543 (URN)10.1021/acsami.2c18956 (DOI)000925320400001 ()36625710 (PubMedID)2-s2.0-85146341807 (Scopus ID)
Available from: 2023-03-03 Created: 2023-03-03 Last updated: 2023-10-09Bibliographically approved
Luchini, A., Tidemand, F. G., Johansen, N. T., Sebastiani, F., Corucci, G., Fragneto, G., . . . Arleth, L. (2022). Dark peptide discs for the investigation of membrane proteins in supported lipid bilayers: the case of synaptobrevin 2 (VAMP2). Nanoscale Advances, 10(17)
Open this publication in new window or tab >>Dark peptide discs for the investigation of membrane proteins in supported lipid bilayers: the case of synaptobrevin 2 (VAMP2)
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2022 (English)In: Nanoscale Advances, E-ISSN 2516-0230, Vol. 10, no 17Article in journal (Refereed) Published
Abstract [en]

Supported lipid bilayers (SLBs) are commonly used as model systems mimicking biological membranes. Recently, we reported a new method to produce SLBs with incorporated membrane proteins, which is based on the application of peptide discs [Luchini et al., Analytical Chemistry, 2020, 92, 1081-1088]. Peptide discs are small discoidal particles composed of a lipid core and an outer belt of self-assembled 18A peptides. SLBs including membrane proteins can be formed by depositing the peptide discs on a solid support and subsequently removing the peptide by buffer rinsing. Here, we introduce a new variant of the 18A peptide, named dark peptide (d18A). d18A exhibits UV absorption at 214 nm, whereas the absorption at 280 nm is negligible. This improves sample preparation as it enables a direct quantification of the membrane protein concentration in the peptide discs by measuring UV absorption at 280 nm. We describe the application of the peptide discs prepared with d18A (dark peptide discs) to produce SLBs with a membrane protein, synaptobrevin 2 (VAMP2). The collected data showed the successful formation of SLBs with high surface coverage and incorporation of VAMP2 in a single orientation with the extramembrane domain exposed towards the bulk solvent. Compared to 18A, we found that d18A was more efficiently removed from the SLB. Our data confirmed the structural organisation of VAMP2 as including both alpha-helical and beta-sheet secondary structure. We further verified the orientation of VAMP2 in the SLBs by characterising the binding of VAMP2 with alpha-synuclein. These results point at the produced SLBs as relevant membrane models for biophysical studies as well as nanostructured biomaterials.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2022
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:mau:diva-55391 (URN)10.1039/d2na00384h (DOI)000855805500001 ()36341300 (PubMedID)2-s2.0-85139258329 (Scopus ID)
Available from: 2022-10-17 Created: 2022-10-17 Last updated: 2023-10-09Bibliographically approved
Del Giudice, R., Paracini, N., Laursen, T., Blanchet, C., Roosen-Runge, F. & Cárdenas, M. (2022). Expanding the Toolbox for Bicelle-Forming Surfactant–Lipid Mixtures. Molecules, 27(21), 7628-7628
Open this publication in new window or tab >>Expanding the Toolbox for Bicelle-Forming Surfactant–Lipid Mixtures
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2022 (English)In: Molecules, ISSN 1431-5157, E-ISSN 1420-3049, Vol. 27, no 21, p. 7628-7628Article in journal (Refereed) Published
Abstract [en]

Bicelles are disk-shaped models of cellular membranes used to study lipid–protein interactions, as well as for structural and functional studies on transmembrane proteins. One challenge for the incorporation of transmembrane proteins in bicelles is the limited range of detergent and lipid combinations available for the successful reconstitution of proteins in model membranes. This is important, as the function and stability of transmembrane proteins are very closely linked to the detergents used for their purification and to the lipids that the proteins are embedded in. Here, we expand the toolkit of lipid and detergent combinations that allow the formation of stable bicelles. We use a combination of dynamic light scattering, small-angle X-ray scattering and cryogenic electron microscopy to perform a systematic sample characterization, thus providing a set of conditions under which bicelles can be successfully formed.

Place, publisher, year, edition, pages
MDPI, 2022
National Category
Biochemistry and Molecular Biology
Research subject
Health and society
Identifiers
urn:nbn:se:mau:diva-55888 (URN)10.3390/molecules27217628 (DOI)000883556400001 ()36364455 (PubMedID)2-s2.0-85141759223 (Scopus ID)
Funder
Swedish Research Council, 2018-03990Swedish Research Council, 2018-04833
Available from: 2022-11-10 Created: 2022-11-10 Last updated: 2024-02-05Bibliographically approved
Luchini, A., Tidemand, F. G., Araya-Secchi, R., Campana, M., Cárdenas, M. & Arleth, L. (2022). Structural model of tissue factor (TF) and TF-factor VIIa complex in a lipid membrane: A combined experimental and computational study. Journal of Colloid and Interface Science, 623, 294-305, Article ID S0021-9797(22)00724-X.
Open this publication in new window or tab >>Structural model of tissue factor (TF) and TF-factor VIIa complex in a lipid membrane: A combined experimental and computational study
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2022 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 623, p. 294-305, article id S0021-9797(22)00724-XArticle in journal (Refereed) Published
Abstract [en]

Tissue factor (TF) is a membrane protein involved in blood coagulation. TF initiates a cascade of proteolytic reactions, ultimately leading to the formation of a blood clot. The first reaction consists of the binding of the coagulation factor VII and its conversion to the activated form, FVIIa. Here, we combined experimental, i.e. quartz crystal microbalance with dissipation monitoring and neutron reflectometry, and computational, i.e. molecular dynamics (MD) simulation, methods to derive a complete structural model of TF and TF/FVIIa complex in a lipid bilayer. This model shows that the TF transmembrane domain (TMD), and the flexible linker connecting the TMD to the extracellular domain (ECD), define the location of the ECD on the membrane surface. The average orientation of the ECD relative to the bilayer surface is slightly tilted towards the lipid headgroups, a conformation that we suggest is promoted by phosphatidylserine lipids, and favours the binding of FVIIa. On the other hand, the formation of the TF/FVIIa complex induces minor changes in the TF structure, and reduces the conformational freedom of both TF and FVIIA. Altogether we describe the protein-protein and protein-lipid interactions favouring blood coagulation, but also instrumental to the development of new drugs.

Place, publisher, year, edition, pages
Elsevier, 2022
Keywords
Membrane proteins, Molecular dynamics simulations, Neutron reflectometry, Peptide discs, QCM-D, Supported lipid bilayers, Tissue factor
National Category
Other Chemistry Topics
Identifiers
urn:nbn:se:mau:diva-52207 (URN)10.1016/j.jcis.2022.04.147 (DOI)000829956000007 ()35594588 (PubMedID)2-s2.0-85130078544 (Scopus ID)
Available from: 2022-06-08 Created: 2022-06-08 Last updated: 2024-02-05Bibliographically approved
Correa, Y., Jansen, M., Blanchet, C., Roosen-Runge, F., Pedersen, J. S. & Cárdenas, M. (2022). Structural studies on LDL from patients with high and low lipoprotein (a). Paper presented at EAS (European Atherosclerosis Society) 2022, Milano 22-25 May. Atherosclerosis, 355, 56-56, Article ID EP164.
Open this publication in new window or tab >>Structural studies on LDL from patients with high and low lipoprotein (a)
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2022 (English)In: Atherosclerosis, ISSN 0021-9150, E-ISSN 1879-1484, Vol. 355, p. 56-56, article id EP164Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
Elsevier, 2022
National Category
Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:mau:diva-55399 (URN)10.1016/j.atherosclerosis.2022.06.394 (DOI)000853696400384 ()
Conference
EAS (European Atherosclerosis Society) 2022, Milano 22-25 May
Available from: 2022-10-17 Created: 2022-10-17 Last updated: 2023-08-23Bibliographically approved
Barriga, H., Cárdenas, M., Hall, S., Hellsing, M., Karlsson, M., Pavan, A., . . . Wolff, M. (2021). A Bibliometric Study on Swedish Neutron Users for the Period 2006–2020. Neutron News, 32(4), 28-33
Open this publication in new window or tab >>A Bibliometric Study on Swedish Neutron Users for the Period 2006–2020
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2021 (English)In: Neutron News, ISSN 1044-8632, E-ISSN 1931-7352, Vol. 32, no 4, p. 28-33Article in journal (Refereed) Published
Place, publisher, year, edition, pages
Taylor & Francis, 2021
National Category
Information Studies
Identifiers
urn:nbn:se:mau:diva-48577 (URN)10.1080/10448632.2021.1999147 (DOI)2-s2.0-85121466533 (Scopus ID)
Available from: 2021-12-29 Created: 2021-12-29 Last updated: 2022-11-17Bibliographically approved
Projects
Nano and micro scale characterization of coatings in relation to their functional properties; Malmö UniversityLipidnanopartikel – proteininteraktioner: Formuleringsoptimering för bättre terapeutisk effekt; Malmö University, Biofilms Research Center for BiointerfacesStructure, Composition and Dynamics of Lipoproteins: How to Get New Clinical Markers for AtherosclerosisNeutron scattering and selective deuteration for elucidating how lipids regulate metabolon formationLipid nanoparticles under shear stress require novel flow SANS sample environment; Malmö University
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0003-0392-3540

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