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  Protein-Based Patterning to Spatially Functionalize Biomimetic Membranes

Reverte-Lopez, M., Gavrilovic, S., Merino-Salomon, A., Eto, H., Relimpio, A. Y., Rivas, G., et al. (2023). Protein-Based Patterning to Spatially Functionalize Biomimetic Membranes. Small Methods, 7(12): 2300173. doi:10.1002/smtd.202300173.

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 Creators:
Reverte-Lopez, Maria1, 2, Author           
Gavrilovic, Svetozar1, 2, Author           
Merino-Salomon, Adrian1, 2, Author           
Eto, Hiromune3, Author
Relimpio, Ana Yaguee3, Author
Rivas, German3, Author
Schwille, Petra1, Author           
Affiliations:
1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              
2IMPRS-ML: Martinsried, Max Planck Institute of Biochemistry, Max Planck Society, ou_3531125              
3external, ou_persistent22              

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Free keywords: VESICLES; DIVISION; DNA; SHAPES; SYSTEMChemistry; Science & Technology - Other Topics; Materials Science; 3D-printing; lipid vesicles; microswimmers; patterning; reaction-diffusion systems; surface functionalization; synthetic biology;
 Abstract: The bottom-up reconstitution of proteins for their modular engineering into synthetic cellular systems can reveal hidden protein functions in vitro. This is particularly evident for the bacterial Min proteins, a paradigm for self-organizing reaction-diffusion systems that displays an unexpected functionality of potential interest for bioengineering: the directional active transport of any diffusible cargo molecule on membranes. Here, the MinDE protein system is reported as a versatile surface patterning tool for the rational design of synthetically assembled 3D systems. Employing two-photon lithography, microswimmer-like structures coated with tailored lipid bilayers are fabricated and demonstrate that Min proteins can uniformly pattern bioactive molecules on their surface. Moreover, it is shown that the MinDE system can form stationary patterns inside lipid vesicles, which allow the targeting and distinctive clustering of higher-order protein structures on their inner leaflet. Given their facile use and robust function, Min proteins thus constitute a valuable molecular toolkit for spatially patterned functionalization of artificial biosystems like cell mimics and microcarriers.

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Language(s): eng - English
 Dates: 2023-12-15
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 001016080700001
DOI: 10.1002/smtd.202300173
 Degree: -

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Title: Small Methods
Source Genre: Journal
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Publ. Info: Weinheim : WILEY-VCH
Pages: - Volume / Issue: 7 (12) Sequence Number: 2300173 Start / End Page: - Identifier: ISSN: 2366-9608
CoNE: https://pure.mpg.de/cone/journals/resource/2366-9608