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  Single Particle Plasmon Sensors as Label-Free Technique To Monitor MinDE Protein Wave Propagation on Membranes

Lambertz, C., Martos, A., Henkel, A., Neiser, A., Kliesch, T.-T., Janshoff, A., et al. (2016). Single Particle Plasmon Sensors as Label-Free Technique To Monitor MinDE Protein Wave Propagation on Membranes. Nano Letters, 16(6), 3540-3544. doi:10.1021/acs.nanolett.6b00507.

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 Creators:
Lambertz, Christina1, Author
Martos, Ariadna2, Author              
Henkel, Andreas1, Author
Neiser, Andreas1, Author
Kliesch, Torben-Tobias1, Author
Janshoff, Andreas1, Author
Schwille, Petra2, Author              
Sönnichsen, Carsten1, Author
Affiliations:
1external, ou_persistent22              
2Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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Free keywords: BACTERIAL-CELL DIVISION; SPATIAL REGULATION; ESCHERICHIA-COLI; GOLD NANOROD; IN-VITRO; SYSTEM; NANOPARTICLES; BIOSENSORS; RESONANCE; PATTERNSChemistry; Science & Technology - Other Topics; Materials Science; Physics; Optical dark-field spectroscopy; gold nanorod; plasmon sensor; Min system; protein coverage; spatiotemporal dynamics;
 Abstract: We use individual gold nanorods as pointlike detectors for the intrinsic dynamics of an oscillating biological system. We chose the pattern forming MinDE protein system from Escherichia coli (E. coli), a prominent example for self organized chemical oscillations of membrane-associated proteins that are involved in the bacterial cell division process. Similar to surface plasmon resonance (SPR), the gold nanorods report changes in their protein surface coverage without the need for fluorescence labeling, a technique we refer to as NanoSPR Comparing the dynamics for fluorescence labeled and unlabeled proteins, we find a reduction of the oscillation period by about 20%. The absence of photobleaching allows us to investigate Min proteins attaching and detaching from lipid coated gold nanorods with an unprecedented bandwidth of 100 ms time resolution and 1 h observation time. The long observation reveals small changes of the oscillation period over time. Averaging many cycles yields the precise wave profile that exhibits the four phases suggested in previous reports. Unexpected from previous fluorescence-based studies, we found an immobile static protein layer not dissociating during the oscillation cycle. Hence, NanoSPR is an attractive label-free real-time technique for the local investigation of molecular dynamics with high observation bandwidth. It gives access to systems, which cannot be fluorescently labeled, and resolves local dynamics that would average out over the sensor area used in conventional SPR

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Nano Letters
  Abbreviation : Nano Lett.
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 16 (6) Sequence Number: - Start / End Page: 3540 - 3544 Identifier: ISSN: 1530-6984
CoNE: https://pure.mpg.de/cone/journals/resource/110978984570403