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  Binding of histidine-tagged molecules to vesicles with DGS-NTA (Ni) anchor lipids

Pramanik, S., Steinkühler, J., Dimova, R., Spatz, J., & Lipowsky, R. (2022). Binding of histidine-tagged molecules to vesicles with DGS-NTA (Ni) anchor lipids. Biophysical Journal (Annual Meeting Abstracts), 121(3): 405-Pos, pp. 82-82. doi:10.1016/j.bpj.2021.11.2332.

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BiophysJ_121_2022_S1_82a.pdf (Any fulltext), 32KB
 
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Pramanik, Shreya, Author
Steinkühler, Jan, Author
Dimova, Rumiana, Author
Spatz, Joachim1, Author              
Lipowsky, Reinhard, Author
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              

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 Abstract: Giant unilamellar vesicles (GUVs) are model systems for biomembranes around cells and organelles. Peripheral proteins on cellular membranes are important for signaling and membrane trafficking. The binding of peripheral proteins to the GUV membrane can be achieved by direct interaction with specific lipids. Histidine tag molecules attach to 1,2-dioleoyl-sn-glycero-3-[(N-(5-amino-1-carboxypentyl)iminodiacetic acid)succinyl] (nickel salt) DGS-NTA (Ni) lipids forming an octahedral co-ordinate complex. DGS-NTA (Ni) lipids have been used in many studies for the biofunctionalization of GUVs but what is missing is a comparison of the different protocols of GUV formation and their efficiency of binding the histidine-tagged molecules. In this study, we have explored different protocols for the preparation of GUVs as well as different solution conditions which affect the binding of two histidine-tagged molecules, green fluorescent protein (GFP) and Fluorescein isothiocyanate (FITC), to the NTA lipids. We observe significant differences in binding depending on the preparation protocol for GUV formation and offer plausible explanation for this behavior. This study is important to explore the effect of asymmetry introduced by proteins attaching only to the outer layer of the GUV.

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Language(s): eng - English
 Dates: 2022-02-11
 Publication Status: Published in print
 Pages: 1
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bpj.2021.11.2332
 Degree: -

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Title: Biophysical Journal (Annual Meeting Abstracts)
  Other : Biophys. J. (Annual Meeting Abstracts)
Source Genre: Journal
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Publ. Info: Bethesda, MD : Biophysical Society
Pages: - Volume / Issue: 121 (3) Sequence Number: 405-Pos Start / End Page: 82 - 82 Identifier: ISSN: 0006-3495
CoNE: https://pure.mpg.de/cone/journals/resource/954925385117_1