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https://hdl.handle.net/10442/19183
Εξειδίκευση τύπου : | Άρθρο σε επιστημονικό περιοδικό |
Τίτλος: | Protein-Rich Rafts in Hybrid Polymer/Lipid Giant Unilamellar Vesicles |
Δημιουργός/Συγγραφέας: | Otrin, Nika Otrin, Lado Bednarz, Claudia Träger, Toni K. Hamdi, Farzad [EL] Καστρίτης, Παναγιώτης[EN] Kastritis, Panagiotis Ivanov, Ivan Sundmacher, Kai |
Ημερομηνία: | 2024 |
Γλώσσα: | Αγγλικά |
ISSN: | 1525-7797 1526-4602 |
DOI: | 10.1021/acs.biomac.3c00972 |
Περίληψη: | Considerable attention has been dedicated to lipid rafts due to their importance in numerous cell functions such as membrane trafficking, polarization, and signaling. Next to studies in living cells, artificial micrometer-sized vesicles with a minimal set of components are established as a major tool to understand the phase separation dynamics and their intimate interplay with membrane proteins. In parallel, mixtures of phospholipids and certain amphiphilic polymers simultaneously offer an interface for proteins and mimic this segregation behavior, presenting a tangible synthetic alternative for fundamental studies and bottom-up design of cellular mimics. However, the simultaneous insertion of complex and sensitive membrane proteins is experimentally challenging and thus far has been largely limited to natural lipids. Here, we present the co-reconstitution of the proton pump bo3 oxidase and the proton consumer ATP synthase in hybrid polymer/lipid giant unilamellar vesicles (GUVs) via fusion/electroformation. Variations of the current method allow for tailored reconstitution protocols and control of the vesicle size. In particular, mixing of protein-free and protein-functionalized nanosized vesicles in the electroformation film results in larger GUVs, while separate reconstitution of the respiratory enzymes enables higher ATP synthesis rates. Furthermore, protein labeling provides a synthetic mechanism for phase separation and protein sequestration, mimicking lipid- and protein-mediated domain formation in nature. The latter means opens further possibilities for re-enacting phenomena like supercomplex assembly or symmetry breaking and enriches the toolbox of bottom-up synthetic biology. |
Τίτλος πηγής δημοσίευσης: | Biomacromolecules |
Τόμος/Κεφάλαιο: | 25 |
Τεύχος: | 2 |
Σελίδες: | 778-791 |
Θεματική Κατηγορία: | [EL] Κυτταρολογία[EN] Cytology [EL] Βιοχημεία[EN] Biochemistry [EL] Νανοτεχνολογία[EN] Nanotechnology |
Λέξεις-Κλειδιά: | Lipids Membranes Peptides and proteins Phase separation Vesicles |
EU Grant identifier: | 101086665 (toP.L.K.) 03Z22HN23 03Z22HI2 03COV04 ZS/2016/04/78115 391498659 |
Κάτοχος πνευματικών δικαιωμάτων: | © 2024 The Authors. Published by American Chemical Society |
Ηλεκτρονική διεύθυνση στον εκδότη (link): | https://doi.org/10.1021/acs.biomac.3c0097 |
Σημειώσεις: | Published as part of Biomacromolecules virtual special issue “Functional Compartmentalized Polymeric Systems - In Honor of Wolfgang Meier”. |
Εμφανίζεται στις συλλογές: | Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο
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