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Updated: May 21, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
Studies on the binding behavior of prodigiosin with bovine hemoglobin by multi-spectroscopic techniques
Abstract:
In this article, the interaction mechanism of prodigiosin (PG) with bovine hemoglobin (BHb) is studied in detail using various spectroscopic technologies. UV-vis absorption and fluorescence spectra demonstrate the interaction process. The Stern-Volmer plot and the time-resolved fluorescence study suggest the quenching mechanism of fluorescence of BHb by PG is a static quenching procedure, and the hydrophobic interactions play a major role in binding of PG to BHb. Furthermore, synchronous fluorescence studies, Fourier transform infrared (FTIR) and circular dichroism (CD) spectra reveal that the conformation of BHb is changed after conjugation with PG.
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