Self-Assembly of Dyestuffs and Proteins
Numerous synthetic, low molecular weight compounds like organic azo-dyestuffes form fiber-like aggregates in aqueous solution in close analogy to the self-assembly of various proteins in living systems. The underlying processes can be regarded as physical polymerisations leading to a structural diversity, just as complex as in case of macromolecular chemistry. Several low molecular weight gelators and dyestuffs, with the cationic dyestuff pseudo-isocynanine chloride (PIC) as the most recent example, have been selected for a detailed investigation of their self-assembly with time-resolved light scattering. These systems are compared with corresponding experiments on the behaviour of Ab-amyloid responsible for the Alzheimer disease or on vimentin, an intermediary filament protein from the cytoskeleton. It is the final goal to unravel general principles of such self-assembly mechanisms which facilitates to control aggregate size and aggregate morphology and to develop synthetic systems in analogy to hierarchical structure formation in nature.
Herzog, B. et al.
Aggregation of Pseudoisocyanine Chloride in Aqueous NaCl Solution
Langmuir (2003) 19, 5223-5232 DOI: 10.1021/la020980w
Witte, T. et al.
Time resolved structure analysis of growing b-amyloid fibers
Journal of Structural Biology (2007) 159, 71-81 DOI: 10.1016/j.jsb.2007.02.006
Michels, R. et al.
Kinetic and Structural Features of a dyestuff Coaggregation Studied by Time Resolved Static Light Scattering
J. Phys. Chem. B (2013) 117, 15165-15175 DOI: 10.1021/jp405206p
Lopez, C. G. et al.
Lateral association and elongation of vimentin intermediate filament proteins: A time-resolved light-scattering study
PNAS (2016) 113, 11152–11157 DOI: 10.1073/pnas.1606372113
Lopez, C. G. et al.
Effect of ionic strength on the structure and elongational kinetics of vimentin filaments
Soft Matter (2018) 14, 8445-8454 DOI: 10.1039/c8sm01007b
Hämisch, B. et al.
Self-Assembly of Fibrinogen in Aequos, Thrombin-Free Solutions of Variable Ionic Strenghts
Langmuir (2019) 35, 12113-12122 DOI: 10.1021/acs.langmuir.9b01515