Inducing Lipid Domains in Membranes by Self‐Assembly of DNA Origami
Abstract Self‐assembly of biological molecules and structures is a fundamental property of life. Whereas most biological functions are based on self‐assembled proteins and protein complexes, the self‐assembly of lipids is important for the spatial organization of heterogeneous cellular reaction envi...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Wiley-VCH
2023-05-01
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| Series: | Advanced Materials Interfaces |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/admi.202202500 |
| _version_ | 1827893245519069184 |
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| author | Nishu Kanwa Svetozar Gavrilovic Gereon A. Brüggenthies Yusuf Qutbuddin Petra Schwille |
| author_facet | Nishu Kanwa Svetozar Gavrilovic Gereon A. Brüggenthies Yusuf Qutbuddin Petra Schwille |
| author_sort | Nishu Kanwa |
| collection | DOAJ |
| description | Abstract Self‐assembly of biological molecules and structures is a fundamental property of life. Whereas most biological functions are based on self‐assembled proteins and protein complexes, the self‐assembly of lipids is important for the spatial organization of heterogeneous cellular reaction environments and to catalyze cooperative interactions on/with membranes. Lipid domains or “rafts”, which are known to selectively recruit proteins, play an important functional role in sorting and trafficking of membrane components between subcellular organelles. However, how the recruitment and interactions of proteins in turn contributes to the formation and turnover of these structures has not been systematically addressed, due to the large variety in membrane–protein features and their spatiotemporal dynamics. The small size and transient nature of lipid domains adds to the complexity in visualizing them in living cells. Here, DNA origami is presented as a programmable tool to mimic protein clustering and assembly on membranes and illustrate how nanometer sized lipid domains coalesce into visible domains upon origami self‐assembly in defined patterns. Hence, the local membrane composition can be efficiently regulated by the self‐assembly of peripheral membrane binders. This reinforces the hypothesis that lipid rafts in cells occur as a result of membrane–protein interactions and, in particular, protein self‐assembly. |
| first_indexed | 2024-03-12T21:51:03Z |
| format | Article |
| id | doaj.art-49a798b5828b425c942265a542eabc55 |
| institution | Directory Open Access Journal |
| issn | 2196-7350 |
| language | English |
| last_indexed | 2024-03-12T21:51:03Z |
| publishDate | 2023-05-01 |
| publisher | Wiley-VCH |
| record_format | Article |
| series | Advanced Materials Interfaces |
| spelling | doaj.art-49a798b5828b425c942265a542eabc552023-07-26T01:40:26ZengWiley-VCHAdvanced Materials Interfaces2196-73502023-05-011015n/an/a10.1002/admi.202202500Inducing Lipid Domains in Membranes by Self‐Assembly of DNA OrigamiNishu Kanwa0Svetozar Gavrilovic1Gereon A. Brüggenthies2Yusuf Qutbuddin3Petra Schwille4Department of Cellular and Molecular Biophysics Max Planck Institute for Biochemistry Am Klopferspitz 18 82152 Planegg GermanyDepartment of Cellular and Molecular Biophysics Max Planck Institute for Biochemistry Am Klopferspitz 18 82152 Planegg GermanyDepartment of Cellular and Molecular Biophysics Max Planck Institute for Biochemistry Am Klopferspitz 18 82152 Planegg GermanyDepartment of Cellular and Molecular Biophysics Max Planck Institute for Biochemistry Am Klopferspitz 18 82152 Planegg GermanyDepartment of Cellular and Molecular Biophysics Max Planck Institute for Biochemistry Am Klopferspitz 18 82152 Planegg GermanyAbstract Self‐assembly of biological molecules and structures is a fundamental property of life. Whereas most biological functions are based on self‐assembled proteins and protein complexes, the self‐assembly of lipids is important for the spatial organization of heterogeneous cellular reaction environments and to catalyze cooperative interactions on/with membranes. Lipid domains or “rafts”, which are known to selectively recruit proteins, play an important functional role in sorting and trafficking of membrane components between subcellular organelles. However, how the recruitment and interactions of proteins in turn contributes to the formation and turnover of these structures has not been systematically addressed, due to the large variety in membrane–protein features and their spatiotemporal dynamics. The small size and transient nature of lipid domains adds to the complexity in visualizing them in living cells. Here, DNA origami is presented as a programmable tool to mimic protein clustering and assembly on membranes and illustrate how nanometer sized lipid domains coalesce into visible domains upon origami self‐assembly in defined patterns. Hence, the local membrane composition can be efficiently regulated by the self‐assembly of peripheral membrane binders. This reinforces the hypothesis that lipid rafts in cells occur as a result of membrane–protein interactions and, in particular, protein self‐assembly.https://doi.org/10.1002/admi.202202500DNA origamilipid membranesphase separationself‐assembly |
| spellingShingle | Nishu Kanwa Svetozar Gavrilovic Gereon A. Brüggenthies Yusuf Qutbuddin Petra Schwille Inducing Lipid Domains in Membranes by Self‐Assembly of DNA Origami Advanced Materials Interfaces DNA origami lipid membranes phase separation self‐assembly |
| title | Inducing Lipid Domains in Membranes by Self‐Assembly of DNA Origami |
| title_full | Inducing Lipid Domains in Membranes by Self‐Assembly of DNA Origami |
| title_fullStr | Inducing Lipid Domains in Membranes by Self‐Assembly of DNA Origami |
| title_full_unstemmed | Inducing Lipid Domains in Membranes by Self‐Assembly of DNA Origami |
| title_short | Inducing Lipid Domains in Membranes by Self‐Assembly of DNA Origami |
| title_sort | inducing lipid domains in membranes by self assembly of dna origami |
| topic | DNA origami lipid membranes phase separation self‐assembly |
| url | https://doi.org/10.1002/admi.202202500 |
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