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REPORT: Molecularly engineering cell-surface interfaces
Dec 16, 2014

Topic:Molecularly engineering cell-surface interfaces
Speaker:Prof. Pascal Jonkheijm
                  Laboratory group of Bioinspired Molecular Engineering
                  MESA+ Institute for Nanotechnology, University of Twente, The Netherlands
Time:2014/12/16 15:00(Tuesday )
Room:A501, Supramolecular Lab
Supramolecular chemistry provides nowadays an excellent prospect to construct reversible biological interfaces that can be employed for supramolecular cell manipulation experiments. Making use of supramolecular chemistry is rewarding to develop functional materials and devices. Knowing the limitations involved in ordering proteins at different length scales will surely hasten developing future applications, supramolecular bionanotechnology being the most prominent. The construction of synthetic supramolecular assemblies of proteins provides an excellent tool to fabricate organized bioactive components at surfaces. I will present new synthetic procedures for site-specific noncovalent anchoring of proteins to surfaces and polymers. Special attention is paid to orientational and conformational aspects at the surface and will be demonstrated. Using concepts of multivalency the interactions between proteins and surfaces can be modulated by design. Many of the protein complexes were patterned on surfaces using microcontact printing or nanolithography and visualized using fluorescence microscopy. Furthermore, supramolecular linkers that are sensitive to remote electrochemical stimuli will be presented, using cucurbituril (CB) and cyclodextrin (CD)-modified surfaces. Electrochemical switching was studied using surface embedded electrodes. Cell release was studied in detail in the case of cell-adhesive peptides and growth factors. Lastly, supramolecular linkers were compared to reversible covalent linkers, using imine chemistry, providing insight in the cell receptor signaling pathway. With the development of reversible bioactive platforms on surfaces serving as a reversible dynamic interfaces to cells, improved scaffolds for tissue regeneration will become in hand. First steps into this directions will be introduced as well.
Research Interest
Research in Jonkheijm’s group aims to develop dynamic chemical strategies to understand, to direct and to manipulate cellular processes with temporal and spatial control. By carefully designing molecular building blocks with programmed dynamics insight in the cellular adhesion, migration and differentiation will be used to make a new generation of smart biomaterials, to fabricate multifunctional biochips and to renew synthetic biology.
Key publications:
1. J. Am. Chem. Soc. 136, 12675-12681 (2014). “A supramolecular host-guest carrier system for growth factors employing VHH fragments”
2. J. Am. Chem. Soc. 136, 100-103 (2014). “On-chip electrophoresis in supported lipid bilayer membranes achieved using low potentials”
3. Chem. Soc. Rev. 43, 4449-4469 (2014). “About supramolecular systems for dynamically probing cells”
4. Angew. Chem. Int. Ed. 53, 3400-3404 (2014). “Dual Stimuli-Responsive Self-Assembled Supramolecular Nanoparticles”
5. Chem. Commun., 50, 15144-15147 (2014). “Optical control over bioactive ligands at supramolecular surfaces”
6. Chem. Commun. 49, 3679-81 (2013). “Supramolecular control over cell adhesion via ferrocene-cucurbit[7]uril host-guest binding on gold surfaces”
7. J. Am. Chem. Soc. 135, 3104-11 (2013). “Oriented protein immobilization using covalent and non-covalent chemistry on a thiol-reactive self-reporting surface”
8. Angew. Chem. Int. Ed. 51, 12233-7 (2012). “A supramolecular system for the electrochemically controlled release of cells”
9. J. Am. Chem. Soc. 134, 19199-206 (2012). “Reversible and oriented immobilization of ferrocene-modified proteins”
10. J. Am. Chem. Soc. 133, 10849-57 (2011). “Probing multivalent interactions in a synthetic host-guest complex by dynamic force spectroscopy”
11. Nature Chem. 3, 317-22 (2011). “Molecular ‘Hop, Skip and Jump’: Surface gradient-driven motion along a receptor interface”



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