Int. J. Mol. Sci. 2013, 14(10), 21189-21201; doi:10.3390/ijms141021189
Article

Multivalent Protein Assembly Using Monovalent Self-Assembling Building Blocks

Laboratory of Chemical Biology and Institute of Complex Molecular Systems, Department of Biomedical Engineering, Eindhoven University of Technology, Den Dolech 2, Eindhoven 5612AZ, The Netherlands
* Author to whom correspondence should be addressed.
Received: 15 August 2013; in revised form: 13 September 2013 / Accepted: 8 October 2013 / Published: 22 October 2013
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Abstract: Discotic molecules, which self-assemble in water into columnar supramolecular polymers, emerged as an alternative platform for the organization of proteins. Here, a monovalent discotic decorated with one single biotin was synthesized to study the self-assembling multivalency of this system in regard to streptavidin. Next to tetravalent streptavidin, monovalent streptavidin was used to study the protein assembly along the supramolecular polymer in detail without the interference of cross-linking. Upon self-assembly of the monovalent biotinylated discotics, multivalent proteins can be assembled along the supramolecular polymer. The concentration of discotics, which influences the length of the final polymers at the same time dictates the amount of assembled proteins.
Keywords: supramolecular polymers; protein-assembly; FRET; multivalency; biotin-streptavidin; self-assembling multivalency

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MDPI and ACS Style

Petkau-Milroy, K.; Sonntag, M.H.; Colditz, A.; Brunsveld, L. Multivalent Protein Assembly Using Monovalent Self-Assembling Building Blocks. Int. J. Mol. Sci. 2013, 14, 21189-21201.

AMA Style

Petkau-Milroy K, Sonntag MH, Colditz A, Brunsveld L. Multivalent Protein Assembly Using Monovalent Self-Assembling Building Blocks. International Journal of Molecular Sciences. 2013; 14(10):21189-21201.

Chicago/Turabian Style

Petkau-Milroy, Katja; Sonntag, Michael H.; Colditz, Alexander; Brunsveld, Luc. 2013. "Multivalent Protein Assembly Using Monovalent Self-Assembling Building Blocks." Int. J. Mol. Sci. 14, no. 10: 21189-21201.

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