The binding of lotus seedpod oligomeric procyanidins (LSOPC) and catechin (a major constituent unit of LSOPC) to bovine serum albumin (BSA) was studied by a fluorescence quenching technique. The results revealed that LSOPC could strongly quench the intrinsic fluorescence of BSA through a static quenching procedure, but catechin could not. The Stern–Volmer quenching constant, K SV, and corresponding thermodynamic parameters, ΔG 0, ΔH 0 and ΔS 0, were calculated. The results of synchronous fluorescence and circular dichroism studies showed that LSOPC could cause a conformational change in BSA. In addition, glucose and metal ions could affect the interaction between LSOPC and BSA.
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Published in Zhurnal Prikladnoi Spektroskopii, Vol. 80, No. 6, pp. 893–900, November–December, 2013.
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Wu, Q., Li, S., Fu, X. et al. Spectroscopic Studies on Binding of Lotus Seedpod Oligomeric Procyanidins to Bovine Serum Albumin. J Appl Spectrosc 80, 884–892 (2014). https://doi.org/10.1007/s10812-014-9860-6
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DOI: https://doi.org/10.1007/s10812-014-9860-6