{"entity": "researcher", "timestamp": "2026-07-19T19:21:51.152Z", "family": "Kabedev", "given": "Aleksei", "initials": "A", "orcid": "0000-0003-3429-3713", "affiliations": ["Department of Pharmacy, Uppsala University, 75123 Uppsala, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/e624e3f5fb13454296e35755f02cf693.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/e624e3f5fb13454296e35755f02cf693"}}, "publications": [{"entity": "publication", "iuid": "b4b851075019493a92376a7fa7aea21e", "links": {"self": {"href": "https://publications.scilifelab.se/publication/b4b851075019493a92376a7fa7aea21e.json"}, "display": {"href": "https://publications.scilifelab.se/publication/b4b851075019493a92376a7fa7aea21e"}}, "title": "Lipid packing contributes to the confinement of caveolae to the plasma membrane", "authors": [{"family": "Larsson", "given": "Elin", "initials": "E", "orcid": "0000-0003-4224-8226", "researcher": {"href": "https://publications.scilifelab.se/researcher/c85534a046a4475b93a04bc59537e4d6.json"}}, {"family": "Kabedev", "given": "Aleksei", "initials": "A", "orcid": "0000-0003-3429-3713", "researcher": {"href": "https://publications.scilifelab.se/researcher/e624e3f5fb13454296e35755f02cf693.json"}}, {"family": "Pace", "given": "Hudson", "initials": "H", "orcid": "0000-0001-5116-2577", "researcher": {"href": "https://publications.scilifelab.se/researcher/92ed46491f9147fc92388c6707204e92.json"}}, {"family": "Lindwall", "given": "Jakob", "initials": "J"}, {"family": "Bano", "given": "Fouzia", "initials": "F", "orcid": "0000-0003-0634-7091", "researcher": {"href": "https://publications.scilifelab.se/researcher/af79c94518a4488ea0bd314793eb808c.json"}}, {"family": "Rae", "given": "James", "initials": "J"}, {"family": "Parton", "given": "Robert G", "initials": "RG", "orcid": "0000-0002-7494-5248", "researcher": {"href": "https://publications.scilifelab.se/researcher/499570ab993a4d0991e93597dc82f32e.json"}}, {"family": "Bergstr\u00f6m", "given": "Christel AS", "initials": "CA", "orcid": "0000-0002-8917-2612", "researcher": {"href": "https://publications.scilifelab.se/researcher/1bb49fc33a4e4b73a4f5b723dcbcd752.json"}}, {"family": "Parmryd", "given": "Ingela", "initials": "I", "orcid": "0000-0003-4834-3611", "researcher": {"href": "https://publications.scilifelab.se/researcher/2c6807c0e1424720aa8a1c6518bced2d.json"}}, {"family": "Bally", "given": "Marta", "initials": "M", "orcid": "0000-0002-5865-8302", "researcher": {"href": "https://publications.scilifelab.se/researcher/923521b36e7746a3979801d0502eb6a9.json"}}, {"family": "Lundmark", "given": "Richard", "initials": "R", "orcid": "0000-0001-9104-724X", "researcher": {"href": "https://publications.scilifelab.se/researcher/3e1b756caa79468dab0f960e43cd61d3.json"}}], "type": "posted-content", "published": "2026-06-22", "journal": {"issn-l": null}, "abstract": null, "doi": "10.7554/elife.108369.2", "pmid": null, "labels": {"Integrated Microscopy Technologies Ume\u00e5": "Service"}, "xrefs": [], "notes": [], "created": "2026-06-24T10:31:30.065Z", "modified": "2026-07-18T18:40:39.538Z"}, {"entity": "publication", "iuid": "027db74b59df4f18bced574effdd0d70", "links": {"self": {"href": "https://publications.scilifelab.se/publication/027db74b59df4f18bced574effdd0d70.json"}, "display": {"href": "https://publications.scilifelab.se/publication/027db74b59df4f18bced574effdd0d70"}}, "title": "Stabilizing Mechanisms of \u03b2-Lactoglobulin in Amorphous Solid Dispersions of Indomethacin.", "authors": [{"family": "Kabedev", "given": "Aleksei", "initials": "A", "orcid": "0000-0003-3429-3713", "researcher": {"href": "https://publications.scilifelab.se/researcher/e624e3f5fb13454296e35755f02cf693.json"}}, {"family": "Zhuo", "given": "Xuezhi", "initials": "X"}, {"family": "Leng", "given": "Donglei", "initials": "D"}, {"family": "Foder\u00e0", "given": "Vito", "initials": "V", "orcid": "0000-0003-2855-0568", "researcher": {"href": "https://publications.scilifelab.se/researcher/53b80c59d18b436f838caf56a4850e63.json"}}, {"family": "Zhao", "given": "Min", "initials": "M"}, {"family": "Larsson", "given": "Per", "initials": "P", "orcid": "0000-0002-8418-4956", "researcher": {"href": "https://publications.scilifelab.se/researcher/bbbfff6798624ab2bd003f0462f1b156.json"}}, {"family": "Bergstr\u00f6m", "given": "Christel A S", "initials": "CAS", "orcid": "0000-0002-8917-2612", "researcher": {"href": "https://publications.scilifelab.se/researcher/1bb49fc33a4e4b73a4f5b723dcbcd752.json"}}, {"family": "L\u00f6bmann", "given": "Korbinian", "initials": "K", "orcid": "0000-0002-8710-6347", "researcher": {"href": "https://publications.scilifelab.se/researcher/87c31a098348431db5fc926835e7c769.json"}}], "type": "journal article", "published": "2022-11-07", "journal": {"title": "Mol. Pharm.", "issn": "1543-8392", "volume": "19", "issue": "11", "pages": "3922-3933", "issn-l": "1543-8384"}, "abstract": "Proteins, and in particular whey proteins, have recently been introduced as a promising excipient class for stabilizing amorphous solid dispersions. However, despite the efficacy of the approach, the molecular mechanisms behind the stabilization of the drug in the amorphous form are not yet understood. To investigate these, we used experimental and computational techniques to study the impact of drug loading on the stability of protein-stabilized amorphous formulations. \u03b2-Lactoglobulin, a major component of whey, was chosen as a model protein and indomethacin as a model drug. Samples, prepared by either ball milling or spray drying, formed single-phase amorphous solid dispersions with one glass transition temperature at drug loadings lower than 40-50%; however, a second glass transition temperature appeared at drug loadings higher than 40-50%. Using molecular dynamics simulations, we found that a drug-rich phase occurred at a loading of 40-50% and higher, in agreement with the experimental data. The simulations revealed that the mechanisms of the indomethacin stabilization by \u03b2-lactoglobulin were a combination of (a) reduced mobility of the drug molecules in the first drug shell and (b) hydrogen-bond networks. These networks, formed mostly by glutamic and aspartic acids, are situated at the \u03b2-lactoglobulin surface, and dependent on the drug loading (>40%), propagated into the second and subsequent drug layers. The simulations indicate that the reduced mobility dominates at low (<40%) drug loadings, whereas hydrogen-bond networks dominate at loadings up to 75%. The computer simulation results agreed with the experimental physical stability data, which showed a significant stabilization effect up to a drug fraction of 70% under dry storage. However, under humid conditions, stabilization was only sufficient for drug loadings up to 50%, confirming the detrimental effect of humidity on the stability of protein-stabilized amorphous formulations.", "doi": "10.1021/acs.molpharmaceut.2c00397", "pmid": "36135343", "labels": {"Bioinformatics Support for Computational Resources": "Service"}, "xrefs": [], "notes": [], "created": "2022-11-09T15:48:31.060Z", "modified": "2024-01-16T13:48:34.481Z"}, {"entity": "publication", "iuid": "3a155e54460049e4aaec26f48262277f", "links": {"self": {"href": "https://publications.scilifelab.se/publication/3a155e54460049e4aaec26f48262277f.json"}, "display": {"href": "https://publications.scilifelab.se/publication/3a155e54460049e4aaec26f48262277f"}}, "title": "Membrane insertion mechanism of the caveola coat protein Cavin1.", "authors": [{"family": "Liu", "given": "Kang-Cheng", "initials": "KC"}, {"family": "Pace", "given": "Hudson", "initials": "H"}, {"family": "Larsson", "given": "Elin", "initials": "E"}, {"family": "Hossain", "given": "Shakhawath", "initials": "S", "orcid": "0000-0001-9556-2695", "researcher": {"href": "https://publications.scilifelab.se/researcher/3ca81ff3e4f84f9cbdeffe0b803d8a0c.json"}}, {"family": "Kabedev", "given": "Aleksei", "initials": "A", "orcid": "0000-0003-3429-3713", "researcher": {"href": "https://publications.scilifelab.se/researcher/e624e3f5fb13454296e35755f02cf693.json"}}, {"family": "Shukla", "given": "Ankita", "initials": "A", "orcid": "0000-0003-2824-2709", "researcher": {"href": "https://publications.scilifelab.se/researcher/f232904e8ef046ec87fb86ea95430bd1.json"}}, {"family": "Jerschabek", "given": "Vanessa", "initials": "V"}, {"family": "Mohan", "given": "Jagan", "initials": "J"}, {"family": "Bergstr\u00f6m", "given": "Christel A S", "initials": "CAS"}, {"family": "Bally", "given": "Marta", "initials": "M", "orcid": "0000-0002-5865-8302", "researcher": {"href": "https://publications.scilifelab.se/researcher/923521b36e7746a3979801d0502eb6a9.json"}}, {"family": "Schwieger", "given": "Christian", "initials": "C", "orcid": "0000-0001-8327-1233", "researcher": {"href": "https://publications.scilifelab.se/researcher/5b495d6a11134588b5f2be725d72ed56.json"}}, {"family": "Hubert", "given": "Madlen", "initials": "M", "orcid": "0000-0002-5908-9535", "researcher": {"href": "https://publications.scilifelab.se/researcher/48acd1c7795b45919bba57a5a9817ea7.json"}}, {"family": "Lundmark", "given": "Richard", "initials": "R", "orcid": "0000-0001-9104-724X", "researcher": {"href": "https://publications.scilifelab.se/researcher/3e1b756caa79468dab0f960e43cd61d3.json"}}], "type": "journal article", "published": "2022-06-21", "journal": {"title": "Proc. Natl. Acad. Sci. U.S.A.", "issn": "1091-6490", "volume": "119", "issue": "25", "pages": "e2202295119", "issn-l": "0027-8424"}, "abstract": "Caveolae are small plasma membrane invaginations, important for control of membrane tension, signaling cascades, and lipid sorting. The caveola coat protein Cavin1 is essential for shaping such high curvature membrane structures. Yet, a mechanistic understanding of how Cavin1 assembles at the membrane interface is lacking. Here, we used model membranes combined with biophysical dissection and computational modeling to show that Cavin1 inserts into membranes. We establish that initial phosphatidylinositol (4, 5) bisphosphate [PI(4,5)P2]-dependent membrane adsorption of the trimeric helical region 1 (HR1) of Cavin1 mediates the subsequent partial separation and membrane insertion of the individual helices. Insertion kinetics of HR1 is further enhanced by the presence of flanking negatively charged disordered regions, which was found important for the coassembly of Cavin1 with Caveolin1 in living cells. We propose that this intricate mechanism potentiates membrane curvature generation and facilitates dynamic rounds of assembly and disassembly of Cavin1 at the membrane.", "doi": "10.1073/pnas.2202295119", "pmid": "35696574", "labels": {"Bioinformatics Support for Computational Resources": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC9231606"}], "notes": [], "created": "2022-11-09T15:49:41.053Z", "modified": "2024-01-16T13:48:36.114Z"}]}