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  Molecular tweezers target a protein–protein interface and thereby modulate complex formation

Trusch, F., Kowski, K., Bravo-Rodriguez, K., Breuck, K., Sowislok, A., Wettig, B., et al. (2016). Molecular tweezers target a protein–protein interface and thereby modulate complex formation. Chemical Communications, 52(98), 14141-14144. doi:10.1039/C6CC08039A.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-11E1-0 Version Permalink: https://hdl.handle.net/21.11116/0000-0005-4CB4-B
Genre: Journal Article

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 Creators:
Trusch, F.1, Author
Kowski, K.2, Author
Bravo-Rodriguez, Kenny3, Author           
Breuck, K.1, Author
Sowislok, A.2, Author
Wettig, B.2, Author
Matena, A.2, Author
Sanchez-Garcia, Elsa3, Author           
Meyer, H.4, Author
Schrader, T.2, Author
Bayer, P.1, Author
Affiliations:
1University of Duisburg-Essen, Research Group Structural and Medicinal Biochemistry, Centre for Medical Biotechnology (ZMB), 45117 Essen, Germany , ou_persistent22              
2University of Duisburg-Essen, Research Group Organic Chemistry, 45117 Essen, Germany , ou_persistent22              
3Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1950289              
4University of Duisburg-Essen, Research Group Molecular Biology I, Centre for Medical Biotechnology (ZMB), 45117 Essen, Germany , ou_persistent22              

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 Abstract: Molecular tweezers for lysine and arginine select a few residues on a protein surface and by their unique complexation mode disrupt a critical protein–protein interaction. Detailed structural information was gained by NMR experiments, strongly supported by QM/MM calculations and further substantiated by ITC, fluorescence anisotropy, ELISA and bio-layer-interference studies.

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Language(s): eng - English
 Dates: 2016-10-052016-11-142016-11-152016-12-21
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/C6CC08039A
 Degree: -

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Title: Chemical Communications
  Other : Chem. Commun.
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 52 (98) Sequence Number: - Start / End Page: 14141 - 14144 Identifier: ISSN: 1359-7345
CoNE: https://pure.mpg.de/cone/journals/resource/954928495413