Abstract
Curli, an extracellular protein fibril produced by certain gram-negative enteric bacteria, is responsible for neuro-degenerative diseases due to spontaneous misfolding of soluble proteins. This study investigates the effect of denaturing agents (Urea, Guanidine Hydrochloride) and varying pH (2–11) on the conformation of Curli protein, isolated from E. coli PHL628, due to changes in the external environment. The study focuses on the changing dynamics of the protein using intrinsic fluorescence property, UV-absorption, fluorescence anisotropic measurements, and extrinsic fluorescence property with the help of interaction with 1-anilinonaphthalene-8-sulphonate (ANS). The data showed that the absorption maximum (λmax) of protein was altered in variation of denaturant concentration and buffer pH. Molecular docking results revealed the interaction of Curli with Urea and GdnHCl, by comparing structural changes. This study determines how denaturants and changes in the external environment cause denaturation or modification in the folded structure of Curli protein and provides insight into binding sites of Curli with denaturants.
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