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  Cobalt(III)-mediated permanent and stable immobilization of histidine-tagged proteins on NTA-functionalized surfaces

Wegner, S., Schenk, F. C., & Spatz, J. P. (2016). Cobalt(III)-mediated permanent and stable immobilization of histidine-tagged proteins on NTA-functionalized surfaces. Chemistry – A European Journal, 22(9), 3156-3162. doi:10.1002/chem.201504465.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-1480-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-7E30-E
Genre: Journal Article

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 Creators:
Wegner, Seraphine1, 2, Author              
Schenk, Franziska C.1, 2, Author              
Spatz, Joachim P.1, 2, Author              
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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Free keywords: biofunctionalization; cobalt; histidine; immobilization; surfaces and interfaces
 Abstract: We present the cobalt(III)-mediated interaction between polyhistidine (His)-tagged proteins and nitrilotriacetic acid (NTA)-modified surfaces as a general approach for a permanent, oriented, and specific protein immobilization. In this approach, we first form the well-established Co(2+) -mediated interaction between NTA and His-tagged proteins and subsequently oxidize the Co(2+) center in the complex to Co(3+) . Unlike conventionally used Ni(2+) - or Co(2+) -mediated immobilization, the resulting Co(3+) -mediated immobilization is resistant toward strong ligands, such as imidazole and ethylenediaminetetraacetic acid (EDTA), and washing off over time because of the high thermodynamic and kinetic stability of the Co(3+) complex. This immobilization method is compatible with a wide variety of surface coatings, including silane self-assembled monolayers (SAMs) on glass, thiol SAMs on gold surfaces, and supported lipid bilayers. Furthermore, once the cobalt center has been oxidized, it becomes inert toward reducing agents, specific and unspecific interactions, so that it can be used to orthogonally functionalize surfaces with multiple proteins. Overall, the large number of available His-tagged proteins and materials with NTA groups make the Co(3+) -mediated interaction an attractive and widely applicable platform for protein immobilization.

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Language(s): eng - English
 Dates: 2015-11-062016-01-252016-02-24
 Publication Status: Published in print
 Pages: 7
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 Table of Contents: -
 Rev. Type: Peer
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Title: Chemistry – A European Journal
  Other : Chem. – Eur. J.
  Other : Chem. Eur. J.
Source Genre: Journal
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Publ. Info: Weinheim, Germany : VCH Verlagsgesellschaft
Pages: - Volume / Issue: 22 (9) Sequence Number: - Start / End Page: 3156 - 3162 Identifier: ISSN: 0947-6539
CoNE: https://pure.mpg.de/cone/journals/resource/954926979058