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  • Title: Studies on the interaction of salvianolic acid B with human hemoglobin by multi-spectroscopic techniques.
    Author: Chen T, Zhu S, Cao H, Shang Y, Wang M, Jiang G, Shi Y, Lu T.
    Journal: Spectrochim Acta A Mol Biomol Spectrosc; 2011 Apr; 78(4):1295-301. PubMed ID: 21277824.
    Abstract:
    The interaction between salvianolic acid B (Sal B) and human hemoglobin (HHb) under physiological conditions was investigated by UV-vis absorption, fluorescence, synchronous fluorescence and circular dichroism spectroscopic techniques. The experimental results indicate that the quenching mechanism of fluorescence of HHb by Sal B is a static quenching procedure, the binding reaction is spontaneous, and the hydrophobic interactions play a major role in binding of Sal B to HHb. Based on Förster's theory of non-radiative energy transfer, the binding distance between Sal B and the inner tryptophan residues of HHb was determined to be 2.64 nm. The synchronous fluorescence experiment revealed that Sal B can not lead to the microenvironmental changes around the Tyr and Trp residues of HHb, and the binding site of Sal B on HHb is located at α(1)β(2) interface of HHb. Furthermore, the CD spectroscopy indicated the secondary structure of HHb is not changed in the presence of Sal B.
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