Copper(II) complexes of salicylaldehydes and 2 hydroxyphenones: Synthesis, Structure,

Μέγεθος: px

Εμφάνιση ξεκινά από τη σελίδα:

Download "Copper(II) complexes of salicylaldehydes and 2 hydroxyphenones: Synthesis, Structure,"

Ευθύμιος Μανωλάς
6 χρόνια πριν
Προβολές:

1 Electronic Supplementary Material (ESI) for RSC Advances. This journal is The Royal Society of Chemistry 2015 Copper(II) complexes of salicylaldehydes and 2 hydroxyphenones: Synthesis, Structure, Thermal decomposition study and Interaction with calf thymus DNA and albumins Ariadne Zianna, George Psomas, Antonios G. Hatzidimitriou, Maria Lalia Kantouri * Department of General and Inorganic Chemistry, Faculty of Chemistry, Aristotle University of Thessaloniki, GR Thessaloniki, Greece Supplementary material S1. Interaction with CT DNA The binding constant, K b, can be obtained by monitoring the changes in the absorbance at the corresponding λ max with increasing concentrations of CT DNA and it is given by the ratio of [DNA] slope to the y intercept in plots versus [DNA], according to the Wolfe Shimer equation ( A f ) [1]: [DNA] [DNA] 1 (eq. S1) (ε ε ) (ε ε ) K (ε ε ) A f b f b where [DNA] is the concentration of DNA in base pairs, ε A = A obsd /[compound], ε f = the extinction coefficient for the free compound and ε b = the extinction coefficient for the compound in the fully bound form. b f S2. Competitive studies with EB The Stern Volmer constant K SV is used to evaluate the quenching efficiency for each compound according to the Stern Volmer equation: Io 1 KSV[Q] (eq. S2) I where Io and I are the emission intensities in the absence and the presence of the quencher, respectively, [Q] is the concentration of the quencher (i.e. complexes 1 6); K SV is obtained from the Io Stern Volmer plots by the slope of the diagram vs [Q]. I * Corresponding author: Tel./fax: , E mail address: lalia@chem.auth.gr (M. Lalia Kantouri)

2 S3. Interaction with serum albumins The extent of the inner filter effect can be roughly estimated with the following formula: I corr meas ( exc )cd 2 ( em )cd 2 I (eq. S3) where I corr = corrected intensity, I meas = the measured intensity, c = the concentration of the quencher, d = the cuvette (1 cm), ε(λ exc ) and ε(λ em ) = the ε of the quencher at the excitation and the emission wavelength, respectively, as calculated from the UV Vis spectra of the complexes [2]. The Stern Volmer and Scatchard graphs are used in order to study the interaction of a quencher with serum albumins. According to Stern Volmer quenching equation [3]: Io =1+ kq τ0[q] =1+ KSV[Q] (eq. S4), I where Io = the initial tryptophan fluorescence intensity of SA, I = the tryptophan fluorescence intensity of SA after the addition of the quencher, k q = the quenching rate constants of SA, K SV = the dynamic quenching constant, τ o = the average lifetime of SA without the quencher, [Q] = the concentration of the quencher, the dynamic quenching constant (K SV, M 1 ) can be obtained by the Io slope of the diagram vs [Q]. From the equation: I K SV = k q τ o (eq. S5) and taking τ o = 10 8 s as fluorescence lifetime of tryptophan in SA, the approximate quenching constant (k q, M 1 s 1 ) is calculated. From the Scatchard equation [3]: I Io nk K [Q] ΔI Io (eq. S6) where n is the number of binding sites per albumin and K is the association binding constant, K (in I M 1 ) is calculated from the slope in plots Io [Q] to the slope [3]. ΔI versus and n is given by the ratio of y intercept Io References [1] A. Wolfe, G. Shimer and T. Meehan, Biochemistry, 1987, 26, [2] L. Stella, A.L. Capodilupo and M. Bietti, Chem. Commun., 2008, [3] Y. Wang, H. Zhang, G. Zhang, W. Tao and S. Tang, J. Luminescence, 2007, 126,

3 Table S1. The HSA constants derived for the free saloh and ketoh and their complexes 1 7. Compound Ksv (M 1 ) Kq (M 1 s 1 ) K (M 1 ) n o vanh 2.52(±0.23) (±0.23) (±0.17) Me saloh 0(±0.15) (±0.15) (±0.12) NO 2 saloh 5.00(±0.46) (±0.46) (±0.09) Cl saloh 5.64(±0.40) (±0.40) (±0.10) Br saloh 2.31(±0.32) (±0.32) (±0.09) bpoh 3.05(±0.19) (±0.19) (±0.12) mpoh 7.67(±0.46) (±0.46) (±0.41) [Cu(o van) 2 H 2 O)]. 0.25H 2 O H 2 O 9(±0.25) (±0.25) (±0.22) [Cu(5 CH 3 salo) 2 ], (±0.54) (±0.54) (±0.48) [Cu(5 NO 2 salo) 2 (CH 3 OH) 2 ], (±0.27) (±0.27) (±0.11) [Cu(5 Cl salo) 2 ], (±0.60) (±0.60) (±0.43) [Cu(5 Br salo) 2 ], (±0.07) (±0.07) (±0.36) [Cu(bpo) 2 ], (±0.64) (±0.64) (±0.12) [Cu(mpo) 2 ]. 2H 2 O, 7. 2H 2 O 3.79(±0.18) (±0.18) (±0.68)

4 Table S2. The BSA constants derived for the free saloh and ketoh and their complexes 1 7. Compound K SV (M 1 ) k q (M 1 s 1 ) K (M 1 ) n o vanh 2.37(±0.13) (±0.13) (±0.10) Me saloh 6.15(±0.58) (±0.58) (±0.27) NO 2 saloh 6.55(±0.17) (±0.17) (±0.07) Cl saloh 6(±0.06) (±0.06) (±0.20) Br saloh 4.63(±0.31) (±0.31) (±0.08) bpoh 9.43(±0.36) (±0.36) (±0.23) mpoh 7.41(±0.46) (±0.46) (±0.17) [Cu(o van) 2 H 2 O)]. 0.25H 2 O, H 2 O 3.33(±0.23) (±0.23) (±0.98) [Cu(5 CH 3 salo) 2 ], (±0.51) (±0.51) (±0.13) [Cu(5 NO 2 salo) 2 (CH 3 OH) 2 ], (±0.43) (±0.43) (±0.20) [Cu(5 Cl salo) 2 ], 4 2(±0.09) (±0.09) (±0.81) [Cu(5 Br salo) 2 ], (±0.29) (±0.29) (±0.06) [Cu(bpo) 2 ], (±0.35) (±0.35) (±0.10) [Cu(mpo) 2 ]. 2H 2 O, 7. 2H 2 O 2.88(±0.14) (±0.14) (±0.23)

5 A A A A (A) , 0d 4, 1d 4, 2d , 0d 4, 1d 4, 2d (nm) (nm) (C) , 0d 6, 1d 6, 2d (D) , 0d 6, 1d 6, 2d (nm) (nm) Figure S1. UV spectra of a DMSO solution of complexes (A) 4 (10 3 M), 4 ( M), (C) 6 (10 3 M) and (D) 6 ( M) during time (0 h, 24 h and 48 h).

6 A A A (A) Complex 2 Complex 2 : buffer = 1:2 Complex 2 : buffer = 1: (nm) Complex 6 Complex 6 : buffer = 1:2 Complex 6 : buffer = 1: (nm) (C) Complex 7 Complex 7 : buffer = 1:2 Complex 7 : buffer = 1: (nm) Figure S2. Visible spectra of 10-3 M DMSO solution of complex (A) 2, 6 and (C) 7 upon addition of buffer solution (150 mm NaCl and 15 mm trisodium citrate at ph 7.0) at diverse ratios.

7 Figure S3. PXRD of complex 5.

8 {[DNA]/( A - f )}x10 7, (M 2 cm) {[DNA]/( A - f )}x10 8, (M 2 cm) {[DNA]/( A - f )}x10 8, (M 2 cm) (A) [DNA]x10 5, (M) [DNA]x10 5, (M) (C) Figure S4. Plot of [DNA]x10 5, (M) [DNA] vs [DNA] for (A) o vanh, 5 Me saloh and (C) mpoh. (ε ε ) A f

9 {[DNA]/( A - f )}x10 8, (M 2 cm) {[DNA]/( A - f )}x10 8, (M 2 cm) {[DNA]/( A - f )}x10 8, (M 2 cm) {[DNA]/( A - f )}x10 8, (M 2 cm) {[DNA]/( A - f )}x10 8, (M 2 cm) {[DNA]/( A - f )}x10 8, (M 2 cm) {[DNA]/( A - f )}x10 8, (M 2 cm) (A) [DNA]x10 5, (M) [DNA]x10 5, (M) (C) -0.5 (D) [DNA]x10 5, (M) [DNA]x10 5, (M) (E) (F) [DNA]x10 5, (M) [DNA]x10 5, (M) (G) [DNA]x10 5, (M) Figure S5. (A) (G) Plot of [DNA] vs [DNA] for complexes 1 7, respectively. (ε ε ) A f

10 I ( A) DNA V (mv) Figure S6. Cyclic voltammogram of 0.4 mm 1/2 dmso/buffer (containing 150 mm NaCl and 15 mm trisodium citrate at ph 7.0) solution of [Cu(5 Me salo) 2 ], 2 in the absence or presence of CT DNA. Scan rate = 100 mv s 1. Supporting electrolyte = buffer solution.

11 I/Io (A) [o-vanh]x10 5, (M) [5-Me-saloH]x10 5, (M) (C) [mpoh]x10 5, (M) Figure S7. Stern Volmer quenching plot of EB bound to CT DNA for (A) o vanh, 5 Me saloh and (C) mpoh.

12 (A) [1]x10 5, (M) [2]x10 5, (M) 4.0 (C) [3]x10 5, (M) (D) [4]x10 5, (M) (E) (F) [5]x10 5, (M) [6]x10 5, (M) (G) [7]x10 5, (M) Figure S8. (A) (G) Stern Volmer quenching plot of EB bound to CT DNA for complexes 1 7, respectively.

13 (A) [o-vanh]x10 5, (M) [5-Me-saloH]x10 5, (M) (C) 2.5 (D) [5-NO 2 -saloh]x10 5, (M) [5-Cl-saloH]x10 5, (M) (E) (F) [5-Br-saloH]x10 5, (M) [bpoh]x10 5, (M) (G) [mpoh]x10 5, (M) Figure S9. Stern Volmer quenching plot of BSA for (A) o vanh, 5 Me saloh, (C) 5 NO 2 saloh, (D) 5 Cl saloh, (E) 5 Br saloh, (F) bpoh and (G) mpoh.

14 (A) [1]x10 5, (M) [2]x10 5, (M) (C) [3]x10 5, (M) (D) [4]x10 5, (M) 2.4 (E) (F) [5]x10 5, (M) [6]x10 5, (M) (G) [7]x10 5, (M) Figure S10. (A) (G) Stern Volmer quenching plot of BSA for complexes 1 7, respectively.

15 (A) [o-vanh]x10 5, (M) [5-Me-saloH]x10 5, (M) (C) (D) [5-NO 2 -saloh]x10 5, (M) [5-Cl-saloH]x10 5, (M) 1.30 (E) (F) [5-Br-saloH]x10 5, (M) [bpoh]x10 5, (M) 1.16 (G) [mpoh]x10 5, (M) Figure S11. Stern Volmer quenching plot of HSA for (A) o vanh, 5 Me saloh, (C) 5 NO 2 saloh, (D) 5 Cl saloh, (E) 5 Br saloh, (F) bpoh and (G) mpoh.

16 (A) [1]x10 5, (M) [2]x10 5, (M) (C) (D) [3]x10 5, (M) [4]x10 5, (M) (E) (F) [5]x10 5, (M) [6]x10 5, (M) (G) [7]x10 5, (M) Figure S12. (A) (G) Stern Volmer quenching plot of HSA for complexes 1 7, respectively.

17 /[mpoh] /[5-Br-saloH] /[bpoh] /[5-NO 2 -saloh] /[5-Cl-saloH] /[o-vanh] /[5-Me-saloH] (A) (C) (D) (E) (F) (G) Figure S13. Scatchard plot of BSA for (A) o vanh, 5 Me saloh, (C) 5 NO 2 saloh, (D) 5 Cl saloh, (E) 5 Br saloh, (F) bpoh and (G) mpoh.

18 /[7] /[5] /[6] /[3] /[4] /[1] /[2] (A) (C) (D) (E) (F) (G) Figure S14. (A) (G) Scatchard plot of BSA for complexes 1 7, respectively.

19 /[mpoh] /[5-Br-saloH] /[bpoh] /[5-NO 2 -saloh] /[5-Cl-saloH] /[o-vanh] /[5-Me-saloH] (A) (C) (D) (E) (F) (G) Figure S15. Scatchard plot of HSA for (A) o vanh, 5 Me saloh, (C) 5 NO 2 saloh, (D) 5 Cl saloh, (E) 5 Br saloh, (F) bpoh and (G) mpoh.

20 /[7] /[5] /[6] /[3] /[4] /[1] /[2] (A) (C) (D) (E) (F) (G) Figure S16. (A) (G) Scatchard plot of HSA for complexes 1 7, respectively.

Σχετικά έγγραφα

Electronic Supplementary Information (ESI)

Electronic Supplementary Material (ESI) for Dalton Transactions. This journal is The Royal Society of Chemistry 2016 Electronic Supplementary Information (ESI) Cytotoxic and antimicrobial effects of indium(iii)