Chem. J. Chinese Universities ›› 2015, Vol. 36 ›› Issue (7): 1254.doi: 10.7503/cjcu20141088
• Articles: Inorganic Chemistry • Previous Articles Next Articles
YANG Shuilan, SONG Pan, SHE Wenjie, YANG Tianlin*()
Received:
2014-12-12
Online:
2015-07-10
Published:
2015-06-03
Contact:
YANG Tianlin
E-mail:yang_tl@nxu.edu.cn
Supported by:
CLC Number:
TrendMD:
YANG Shuilan, SONG Pan, SHE Wenjie, YANG Tianlin. Mechanism of the Interaction Between a Phosphorus-containing Tripod Ligand Europium(Ⅲ) Complex and Bovine Serum Albumin†[J]. Chem. J. Chinese Universities, 2015, 36(7): 1254.
Fig.2 Fluorescence emission spectra of BSA influenced by different concentrations of Eu(pic)3LT=303 K, pH=7.3, λex=280 nm, cBSA=1×10-7 mol/L. 107cEu(pic)3L/(mol·L-1) from a to i: 0, 1.0, 2.0, 3.0, 4.0, 5.0, 6.0, 7.0, 8.0.
T/K | 10-5 KSV/(L·mol-1) | 10-13Kq/(L·mol-1·s-1) | R2 |
---|---|---|---|
293 | 4.16 | 4.16 | 0.996 |
303 | 3.88 | 3.88 | 0.993 |
313 | 3.15 | 3.15 | 0.995 |
323 | 3.10 | 3.10 | 0.996 |
Table 1 KSV and kq data of Eu(pic)3L complex-BSA system at different temperatures
T/K | 10-5 KSV/(L·mol-1) | 10-13Kq/(L·mol-1·s-1) | R2 |
---|---|---|---|
293 | 4.16 | 4.16 | 0.996 |
303 | 3.88 | 3.88 | 0.993 |
313 | 3.15 | 3.15 | 0.995 |
323 | 3.10 | 3.10 | 0.996 |
T/K | Equation | K/(L·mol-1) | R2 | n |
---|---|---|---|---|
293 | lg(F0/F-1)=6.57+1.33lgcQ | 1.24×106 | 0.991 | 1.33 |
303 | lg(F0/F-1)=6.39 +1.30lgcQ | 2.88×105 | 0.993 | 1.30 |
313 | lg(F0/F-1)=6.14+1.26lgcQ | 1.51×105 | 0.994 | 1.26 |
323 | lg(F0/F-1)=5.82+1.21lgcQ | 4.11×104 | 0.994 | 1.21 |
Table 2 Binding constants(K), binding sites(n) and R2 of Eu(pic)3L complex-BSA at different temperatures
T/K | Equation | K/(L·mol-1) | R2 | n |
---|---|---|---|---|
293 | lg(F0/F-1)=6.57+1.33lgcQ | 1.24×106 | 0.991 | 1.33 |
303 | lg(F0/F-1)=6.39 +1.30lgcQ | 2.88×105 | 0.993 | 1.30 |
313 | lg(F0/F-1)=6.14+1.26lgcQ | 1.51×105 | 0.994 | 1.26 |
323 | lg(F0/F-1)=5.82+1.21lgcQ | 4.11×104 | 0.994 | 1.21 |
T/K | ΔH/(kJ·mol-1) | ΔS/(J·K-1) | ΔG/(kJ·mol-1) |
---|---|---|---|
293 | -107.76 | -251.13 | -34.19 |
303 | -107.76 | -251.12 | -31.67 |
313 | -107.76 | -245.14 | -31.03 |
323 | -107.76 | -245.29 | -28.53 |
Table 3 Thermodynamic parameters of complex-BSA binding procedure
T/K | ΔH/(kJ·mol-1) | ΔS/(J·K-1) | ΔG/(kJ·mol-1) |
---|---|---|---|
293 | -107.76 | -251.13 | -34.19 |
303 | -107.76 | -251.12 | -31.67 |
313 | -107.76 | -245.14 | -31.03 |
323 | -107.76 | -245.29 | -28.53 |
Fig.8 Quenching effect of Eu(pic)3L complex on BSA fluorescence in the presence of Cu2+(A) and Fe3+(B) T=303 K, pH=7.3, λex=280 nm, cCu2+-BSA or cFe3+-BSA=1×10-6 mol/L. 107cEu(pic)3L/(mol·L-1): a. 0; b. 1.0; c. 2.0; d. 3.0; e. 4.0; f. 5.0; g. 6.0; h. 7.0; i. 8.0; j. 9.0.
Fig.9 Stern-Volmer curves(A) and double logarithm plots(B) showing the Eu(pic)3L complex quenching effect on BSA fluorescence in the presence of Fe3+ and Cu2+ ions respectively(B)
System | K/(L·mol-1) | n | R2 |
---|---|---|---|
Complex-BSA | 2.88×105 | 1.30 | 0.993 |
Complex-BSA-Cu2+ | 9.98×106 | 1.31 | 0.992 |
Complex-BSA-Fe3+ | 1.79×106 | 1.38 | 0.998 |
Table 4 Binding parameters of Eu(pic)3L complex-BSA system in the presence of Fe3+ and Cu2+
System | K/(L·mol-1) | n | R2 |
---|---|---|---|
Complex-BSA | 2.88×105 | 1.30 | 0.993 |
Complex-BSA-Cu2+ | 9.98×106 | 1.31 | 0.992 |
Complex-BSA-Fe3+ | 1.79×106 | 1.38 | 0.998 |
Fig.11 CV curves of Eu(pic)3L complex with DNA(A) and the plot of 1/(1-i/i0) vs 1/cBSA(B)cEu(pic)3L=1×10-5 mol/L. cBSA/(10-6 mol·L-1) form a to f: 0; 1.0; 2.0; 3.0; 4.0; 5.0.
System | T/K | 10-5Kb/(L·mol-1) | R2 |
---|---|---|---|
Complex-BSA | 293 | 1.57 | 0.996 |
Complex-BSA | 303 | 3.28 | 0.998 |
Table 5 Kb of Eu(pic)3L complex and BSA at different temperatures
System | T/K | 10-5Kb/(L·mol-1) | R2 |
---|---|---|---|
Complex-BSA | 293 | 1.57 | 0.996 |
Complex-BSA | 303 | 3.28 | 0.998 |
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