ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022
A Quick and Reproducible Silanization Method by Using Plasma Activation for Hydrophobicity-Based Kinesin Single Molecule Fluorescence-Microscopy Assays.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- The tail domain of the plant kinesin-12 POK2 is a versatile interaction hub.Journal of cell science · 2025Article
- Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays.Cytoskeleton (Hoboken, N.J.) · 2025Article
- NuMA is a mitotic adaptor protein that activates dynein and connects it to microtubule minus ends.The Journal of cell biology · 2025Article
- Selective regulation of kinesin-5 function by β-tubulin carboxy-terminal tails.The Journal of cell biology · 2025Article
- Structural basis of MICAL autoinhibition.Nature communications · 2024Article
- Microtubule binding of the human augmin complex is directly controlled by importins and Ran-GTP.Journal of cell science · 2023Article
- A Quick and Reproducible Silanization Method by Using Plasma Activation for Hydrophobicity-Based Kinesin Single Molecule Fluorescence-Microscopy Assays.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Single-molecule assays often require functionalized surfaces. One approach for microtubule assays renders surfaces hydrophobic and uses amphiphilic blocking agents. However, the optimal hydrophobicity is unclear, protocols take long, produce toxic waste, and are susceptible to failure. Our method uses plasma activation with hydrocarbons for hexamethyldisilazane (HMDS) silanization in the gas phase. We measured the surface hydrophobicity, its effect on how well microtubule filaments were bound to the surface, and the number of nonspecific interactions with kinesin motor proteins. Additionally, we tested and discuss the use of different silanes and activation methods. We found that even weakly hydrophobic surfaces were optimal. Our environmentally friendly method significanty reduced the overall preparation effort and resulted in reproducible, high-quality surfaces with low variability. We expect the method to be applicable to a wide range of other single-molecule assays.
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Registered trials
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