Research project The project aims at a molecular-level-development of polarised light spectroscopy for insights into complex biostructures, in particular the dynamics, structure and functioning of proteins, as related to the folding and formation of regular protein aggregates (= non-covalent polymers). The studies of protein aggregation are related to fibrinolytic activity, amyloid diseases, actin polymerisation and pore-forming cytotoxins. In another branch of the project, enhanced fluorescence is studied for the development of amplifiers of chemical sensors, which can be used in e.g. point-of-care analysis.
For decades fluorescence resonance energy transfer (FRET) has been applied in studies of protein structure. From a physical point of view it is more enlightening to refer to the process as “resonance energy transfer” (RET) or “donor-acceptor energy transfer” (DAET), since the mechanism is a non-radiative process between electronic states. The application of RET on biosystems requires the specific insertion of a donor and an acceptor group into a structure, which turns out to be a fundamental limitation of the RET-method. However, this and other limitations of RET are circumvented by the work done within this project. It has been demonstrated that the use of two identical fluorescent groups solves the question of specificity, and also that chemically identical but photophysically non-identical groups can be used for obtaining quantitative distance information. Furthermore Förster's theory of RET is not valid for a detailed molecular analysis of experiments on most biomacromolecular systems. The extended Förster theory (EFT) developed within this project intends to bring the analyses of experiments to the same level of molecular description as in ESR and NMR spectroscopy. Hitherto this strive has been very promising.