Study of the interaction between icariin and human serum albumin by fluorescence spectroscopy

Zhang, Guowen; Que, Qingmin; Pan, Junhui; Guo, Jinbao

doi:10.1016/j.molstruc.2007.09.002

Cited by 295 publications

(136 citation statements)

References 34 publications

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“…Therefore, the shift of the maximum emission wavelength reveals the alteration of molecule. The synchronous fluorescence can provide the characteristic information of the Try or Trp residues when the Δλ value between excitation and emission wavelength is set at 15 or 60 nm [1,22].…”

Section: Effect Of Lour B On the Hsa Conformationmentioning

confidence: 99%

Fluorescence study on the interaction of human serum albumin with loureirin B

Yong

et al. 2010

Spectroscopy

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Abstract. The interaction between loureirin B (Lour B) and human serum albumin (HSA) was investigated by fluorescence and UV-vis absorption spectroscopy. Experimental results indicated that loureirin B had a strong ability to quench the intrinsic fluorescence of HSA through a dynamic quenching procedure. The fluorescence quenching data revealed that the quenching constants (K SV ) 2.68 × 10 4 , 3.30 × 10 4 and 4.10 × 10 4 l/mol at 300, 310 and 320 K, respectively. Based on the thermodynamic parameters obtained, the positive values of enthalpy change ΔH and entropy change ΔS suggested that hydrophobic forces played a major role in the interaction of Lour B with HSA. According to Förster theory of energy transfer, the distance r between HSA and Lour B was calculated to be 2.85 nm. Furthermore, the effect of Lour B on the conformation of HSA was analyzed by synchronous fluorescence and three-dimensional fluorescence spectra.

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Section: Effect Of Lour B On the Hsa Conformationmentioning

confidence: 99%

Fluorescence study on the interaction of human serum albumin with loureirin B

Yong

et al. 2010

Spectroscopy

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“…8,9 Lanthanum chloride caused changes in the lipid peroxidation, the redox system and the ATPase activities in the plasma membranes of the rice seeding roots. 10,11 Lanthanum carbonate was approved as a medication (Fosrenol, Shire Pharmaceuticals) to absorb excess phosphate in cases of end-stage renal failure. Some rare-earth chlorides, such as lanthanum chloride (LaCl 3 ), are known to have anticoagulant properties.…”

Section: 2mentioning

confidence: 99%

A Thermodynamic Study on the Binding of Human Serum Albumin with Lanthanum Ion

et al. 2010

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Thermodynamics of the interaction between lanthanum(III) ion, La 3＋ , and human serum albumin (HSA), was investigated at pH 7.0 and 300 K in Tris-HCl buffer by isothermal titration calorimetry. A solvation model was used to reproduce the enthalpies of HSA interaction with La 3＋ . The solvation parameters recovered from our new model were attributed to the structural change of HSA and its biological activity. The interaction of HSA with La 3＋showed a set of two binding sites with negative cooperativity.

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“…The crystallographic analysis of HSA revealed that this protein is a single-chain 66 kDa protein, which is largely α-helical, and consists of three structurally homologous domains that assemble to form a heartshaped molecule. Each domain is a product of two subdomains, which are predominantly helical and extensively cross-linked by several disulfide bridges [10][11][12][13] .…”

Section: Introductionmentioning

confidence: 99%

A Thermodynamic Study on the Binding of Human Serum Albumin with New synthesized Anticancer Pd(II) Complex

Behbehani¹,

Barzegar²

2012

Orientjchem.

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The thermodynamics interaction between new synthesized anti-cancer drugcomplex, Pd 2 Py 2 , and HSA wasinvestigated at pH 7 by isothermal titration calorimetry. The extended solvation model was used to reproduce the enthalpies of HSA interaction withPd 2 Py 2 . The solvation parameters obtained from the new model was attributed to the structural change and anti-oxidant property of HSA. The binding parameters for the interaction of Pd 2 Py 2 and HSA indicated that the considerable conformational changes in HSA were not observed after binding toPd 2 Py 2 .

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Study of the interaction between icariin and human serum albumin by fluorescence spectroscopy

Cited by 295 publications

References 34 publications

Fluorescence study on the interaction of human serum albumin with loureirin B

Fluorescence study on the interaction of human serum albumin with loureirin B

A Thermodynamic Study on the Binding of Human Serum Albumin with Lanthanum Ion

A Thermodynamic Study on the Binding of Human Serum Albumin with New synthesized Anticancer Pd(II) Complex

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