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This study surveys the rutin (RTN) effect on the thermal denaturation and aggregation of bovine hemoglobin (BHb) under in vitro physiological incubation conditions using differential scanning microcalorimetry (μDSC), circular dichroism (CD), dynamic light scattering (DLS), and atomic force microscopy (AFM). Molecular docking and fractal analysis of AFM imagines support the results obtained using CD and DLS. Higher ordered fibrils occurred for long time incubated BHb, as opposed to lower ordered structures and protofibrils in the presence of RTN. The polyphenol exerts a concentration-dependent effect on the aggregation of BHb, inhibits the growth of fibril-like protein structures and promotes the formation of disordered aggregates or protofibrils. These findings may offer valuable insights in polyphenol-protein interaction, with applications in biochemistry, biophysics, and pharmaceutical research. • RTN modulates the aggregation of BHb, in a concentration-dependent manner. • AFM images reveal the formation of fibril-like structures in free BHb. • RTN prevents the growth of fibril-like protein structures. • RTN promotes the formation of disordered aggregates. • μDSC, CD and DLS data point to the unbound solvated RTN as aggregation promotor.
Precupaş et al. (Tue,) studied this question.
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