Abstract
Serpin (serine protease inhibitor) is a structural prototype for the study of the molecular mechanism of many diseases due to the conformational instability which leads to protein aggregation. The inhibitory function of serpin relys on a flexible loop undertaking a striking conformational transition, but this property also leaves serpin at risk of polymerization. We have investigated the conformational dynamics of the reaction center loop (RCL) of the plasminogen activator inhibitor-1 (PAI-1) by time resolved fluorescence spectroscopy. The RCL becomes more solvent exposed and exhibits faster rotation when PAI-1 interacts with an octapeptide which blocks the loop insertion pathway, indicating that the RCL is well displaced from the protein surface. A heterogeneous population model with three rotational correlation times has been developed to account for the “dip and rise” observed in fluorescence anisotropy decays. We have also employed single molecule FRET to probe the conformational change of serpin under different environment and the early stage of its ploymerization process. Preliminary results will be presented.
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