Lecture I.K. Voets
|17 June 2011||FWN-Building 5111.0006, Nijenborgh 4, 9747 AG, Groningen|
|Speaker:||Dr. I.K. Voets|
|Affiliation:||Dept. of Chemical Engineering and Chemistry, Eindhoven University of Technology|
|Title:||Self-assembly of polymers into complex hierarchical structures|
|Date:||Fri Jun 17, 2011|
|Telephone:||+31 50 363 6867|
Hierarchical assemblies of polymers form via a wide variety of equilibrium and out-of-equilibrium routes giving rise to nanostructured objects with complex structural and dynamical properties. For example, electrostatically driven co-assembly of two oppositely charged double hydrophilic block copolymers in aqueous solutions results in core-shell micelles with a mixed core, consisting of polyelectrolyte blocks, and a mixed corona, consisting of neutral solvent-swollen blocks. The miscibility of the shell-forming blocks, and thereby the extent of chain mixing /segregation in the micellar corona, can be tuned by, for example, segment chemistry and solvent quality, yielding so-called onion-type, Janus-type, and raspberry-like micelles depending on the relative abundance and compatibility of the polymer blocks.
Aggregates of protein molecules are another intriguing example of complex polymer assemblies. In vivo, they may be anything from vital - think of for example actin and tubulin polymerization - to rather detrimental as is the case in protein condensation diseases, such as sickle cell anaemia, cataract, and Alzheimer's disease. In food and other industries, control over protein stability, aggregation, and gelation is necessary in the development of products with a desired appearance, texture, taste, and function. To better understand and ultimately control how proteins fold, unfold, and aggregate, we study solvent-induced self-organization of proteins and protein-like polymers, that is, copolymers grafted with “sticky” side chains that promote folding and “stabilizing” moieties that ensure solubility.
|Last modified:||22 October 2012 2.30 p.m.|