Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Design
and
Synthesis
Chemodosimetric
of
Heterobimetallic
Ensembles
for
the
Donor-Acceptor
Detection
of
Sulfhydryl-Containing Amino Acids and Peptides
Cheuk-Fai Chowa, Hongyan Suia, Michael H. W. Lam*a, Wai-Yeung Wongb
a
Department of Biology & Chemistry, City University of Hong Kong, 83 Tat Chee Ave.,
Hong Kong SAR, China
b
Department of Chemistry, Hong Kong Baptist University, Waterloo Road, Kowloon Tong,
Hong Kong SAR, China
Supplementary Information
Figure S1 - Typical absorption spectra of cis-FeII(bpy)2(CN)2 (-----) and
cis-{FeII(bpy)2[CNPt(DMSO)Cl2]2} (1) () in aqueous DMF (1:1 v/v) (pH 7) at
room temperature.
-1
-1
3
Molar absorption coefficient (cm mol dm )
6000
4000
2000
0
300
400
500
Wavelength (nm)
600
700
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Figure
S2
–
Absorption
spectra
of
cis-RuII(bpy)2(CN)2
(-----)
and
cis-{RuII(bpy)2[CNPt(DMSO)Cl2]2} (2) () in aqueous DMF (1:1 v/v) (pH 7) at
room temperature.
3
Molar absorption coefficient (cm mol dm )
12000
-1
-1
10000
8000
6000
4000
2000
0
300
400
500
Wavelength (nm)
600
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Figure S3 – Typical luminescent spectra of cis-RuII(bpy)2(CN)2 (-----) and
cis-{RuII(bpy)2[CNPt(DMSO)Cl2]2} (2) () in aqueous DMF (1:1 v/v) (pH 7) at
room temperature. Emission spectra were obtained with 467 nm excitation.
3000000
Emission intensity (A.U.)
2500000
2000000
1500000
1000000
500000
0
500
550
600
650
700
Wavelength (nm)
750
800
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Figure
S4
–
Absorption
spectra
of
cis-OsII(bpy)2(CN)2
(-----)
and
cis-{OsII(bpy)2[CNPt(DMSO)Cl2]2} (3) () in aqueous DMF (1:1 v/v) (pH 7) at
room temperature.
8000
-1
-1
3
Molar absorption coefficient (cm mol dm )
10000
6000
4000
2000
0
300
400
500
600
Wavelength (nm)
700
800
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Figure S5 – (i) Electrospray mass spectra of cis-{FeII(bpy)2[CNPt(DMSO)Cl2]2}
(1) in aqueous DMF (1:1 DMF:pH 7 v/v). (ii) Isotopic distribution of ES-MS of the
[M+DMF-Cl]+ peak of (1) (C29FeH35N7O3S2Cl3Pt2) at m/z 1146 in aqueous DMF (1:1
DMF:pH 7 v/v).
1500000
1000000
1146 m/z (M+DMF-Cl)
500000
0
0
200
400
600
800
1000
1200
1400
1600
1800
2000
Mass to charge ratio (M/Z)
(i)
simulation of the
250000
[M+DMF-Cl]+
(C29FeH35N7O3S2Cl3Pt2)
200000
at m/z 1146.
Relative Intensity (A.U.)
Relative Intensity (A.U.)
2000000
150000
100000
50000
0
1135
1140
1145
1150
Mass to charge ratio (M/Z)
(ii)
1155
1160
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Figure S6 – (i) Electrospray mass spectra of cis-{RuII(bpy)2[CNPt(DMSO)Cl2]2}
(2) in aqueous DMF (1:1 DMF:pH 7 v/v). (ii) Isotopic distribution of ES-MS of the
[M-Cl]+ peak of (2) (C26H28N6O2S2Cl3RuPt2) at m/z 1118 in aqueous DMF (1:1
DMF:pH 7 v/v).
500000
1118 m/z (M-Cl)
Relative Intensity (A.U.)
400000
1040 m/z (M-Cl-DMSO)
300000
200000
100000
0
0
200
400
600
800
1000
1200
1400
1600
1800
2000
Mass to charge ratio (M/Z)
(i)
simulation of the [M-Cl]+
(C26H28N6O2S2Cl3RuPt2)
800000
at m/z 1118
Relative Intensity (A.U.)
700000
600000
500000
400000
300000
200000
100000
0
1105
1110
1115
1120
1125
Mass to charge ratio (M/Z)
(ii)
1130
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Figure S7 – (i) Electrospray mass spectra of cis-{OsII(bpy)2[CNPt(DMSO)Cl2]2}
(3) in aqueous DMF (1:1 DMF:pH 7 v/v). (ii) Isotopic distribution of ES-MS of the
[M+DMF-Cl]+ peak of (3) (C29H35N7O3OsS2Cl3Pt2) at m/z 1280 in aqueous DMF (1:1
DMF:pH 7 v/v).
400000
1280 m/z (M+DMF-Cl)
200000
100000
0
200
0
400
600
800
1000
1200
1400
1600
1800
2000
Mass to charge ratio (M/Z)
(i)
simulation of the
[M+DMF-Cl]+
120000
(C29H35N7O3OsS2Cl3Pt2)
110000
at m/z 1280.
100000
90000
Relative Intensity (A.U.)
Relative Intensity (A.U.)
300000
80000
70000
60000
50000
40000
30000
20000
10000
0
1265
1270
1275
1280
1285
Mass to charge ratio (M/Z)
(ii)
1290
1295
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Figure S8 – Responses of the in-situ formed donor-acceptor ensembles to common amino acids and GSH. E5 represents the
{cis-[RuII(bpy)2(CN)2] + CrCl3} ensemble; E6 represents the {cis-[RuII(bpy)2(CN)2] + MnCl2} ensemble; E7 represents the
{cis-[RuII(bpy)2(CN)2] + CoCl2}; E8 represents the {cis-[RuII(bpy)2(CN)2] + NiCl2} ensemble; E9 represents the {cis-[RuII(bpy)2(CN)2] +
CuCl2} ensemble; E10 represents the {cis-[RuII(bpy)2(CN)2] + ZnCl2} ensemble.
1200000
2200000
400000
300000
200000
E5
100000
2000000
All amino acids/
peptide unchange
the ensemble's
luminescent.
1800000
Emission intensity (A.U.)
Enhancement with every
amino acids/peptide
500000
1600000
1400000
1200000
1000000
800000
E6
600000
400000
200000
(E6)
(E6) + GSH
(E6) + Hcys
(E6) + Cys
(E6) + Met
(E6) + His
(E6) + Ser
(E6) + Asp
(E6) + Glu
(E6) + Arg
(E6) + Gly
(E6) + Ala
(E6) + Val
(E6) + Leu
(E6) + Asn
(E6) + Gln
(E6) + Lys
(E6) + Phe
(E6) + Pro
1000000
S10
(E7)
(E7) + GSH
(E7) + Hcys
(E7) + Cys
(E7) + Met
(E7) + His
(E7) + Ser
(E7) + Asp
(E7) + Glu
(E7) + Arg
(E7) + Gly
(E7) + Ala
(E7) + Val
(E7) + Leu
(E7) + Asn
(E7) + Gln
(E7) + Lys
(E7) + Phe
(E7) + Pro
E7
800000
600000
GSH, Hcys,
Cys and His
400000
200000
0
0
500
550
600
650
700
750
0
500
800
550
600
650
700
750
500
800
550
600
650
700
750
800
Wavelength (nm)
Wavelength (nm)
Wavelength (nm)
1200000
1200000
1800000
600000
400000
E8
200000
0
500
550
600
650
700
Wavelength (nm)
750
800
1600000
1400000
Enhancement with every
amino acids/peptide
1200000
1000000
800000
600000
400000
E9
200000
0
500
(E9)
(E9) + GSH
(E9) + Hcys
(E9) + Cys
(E9) + Met
(E9) + His
(E9) + Ser
(E9) + Asp
(E9) + Glu
(E9) + Arg
(E9) + Gly
(E9) + Ala
(E9) + Val
(E9) + Leu
(E9) + Asn
(E9) + Gln
(E9) + Lys
(E9) + Phe
(E9) + Pro
1000000
Emission intensity (A.U.)
Enhancement with every
amino acids/peptide
800000
(E8)
(E8) + GSH
(E8) + Hcys
(E8) + Cys
(E8) + Met
(E8) + His
(E8) + Ser
(E8) + Asp
(E8) + Glu
(E8) + Arg
(E8) + Gly
(E8) + Ala
(E8) + Val
(E8) + Leu
(E8) + Asn
(E8) + Gln
(E8) + Lys
(E8) + Phe
(E8) + Pro
Emission intensity (A.U.)
1000000
Emission intensity (A.U.)
Emission intensity (A.U.)
600000
(E5)
(E5) + GSH
(E5) + Hcys
(E5) + Cys
(E5) + Met
(E5) + His
(E5) + Ser
(E5) + Asp
(E5) + Glu
(E5) + Arg
(E5) + Gly
(E5) + Ala
(E5) + Val
(E5) + Leu
(E5) + Asn
(E5) + Gln
(E5) + Lys
(E5) + Phe
(E5) + Pro
Emission intensity (A.U.)
700000
Enhancement with every
amino acids/peptide
800000
600000
400000
S13
E10
200000
0
550
600
650
700
Wavelength (nm)
750
800
500
550
600
650
700
Wavelength (nm)
750
800
(E10)
(E10) + GSH
(E10) + Hcys
(E10) + Cys
(E10) + Met
(E10) + His
(E10) + Ser
(E10) + Asp
(E10) + Glu
(E10) + Arg
(E10) + Gly
(E10) + Ala
(E10) + Val
(E10) + Leu
(E10) + Asn
(E10) + Gln
(E10) + Lys
(E10) + Phe
(E10) + Pro
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Figure S9 – Spectroscopic titration of Pt(DMSO)2Cl2 (2  10-5 M) with common amino acids and GSH in aqueous DMF (buffered at pH 7 by
HEFES), ionic strength = 0.01 M, at 25 C. For GSH and Hcys, change in absorbance at 275 nm was monitored. For Ala, Asn, Gln, Ser and Val,
change in absorbance at 295 nm was monitored. For Asp, His, Glu, Gly, Leu, Lys, Met, Phe and Pro, change in absorbance at 325 nm was
monitored. For Arg, change in absorbance at 395 nm was monitored.
0.6
0.5
0.4
0.5
0.4
0.3
2
R = 0.995
0.3
2
R = 0.996
AO/(A - AO)
2
AO/(A - AO)
AO/(A - AO)
0.4
0.3
0.2
R = 0.992
0.2
0.2
0.1
0.1
0.1
0.0
0.0
0
50000
100000
150000
200000
250000
300000
0.0
0
350000
50000 100000 150000 200000 250000 300000 350000 400000 450000
0
50000
100000 150000 200000 250000 300000 350000 400000
1/[Hcys]
1/[GSH]
-7
1/[Cys]
-12
-6
-14
-12
-10
-5
-10
-8
-3
AO/(A - AO)
-4
AO/(A - AO)
AO/(A - AO)
2
R = 0.997
2
R = 0.999
-6
-4
-2
-8
2
R = 0.999
-6
-4
-2
-1
0
-2
0
0
20000
40000
60000
1/[Met]
80000
100000
120000
0
0
1000
2000
1/[His]
3000
4000
0
1000
2000
1/[Leu]
3000
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
-14
-14
-14
-12
-12
-12
-10
-10
-10
2
R = 0.994
-6
-8
AO/(A - AO)
-8
AO/(A - AO)
AO/(A - AO)
Figure S9 – Spectroscopic titration of Pt(DMSO)2Cl2 (2  10-5 M) with common amino acids and GSH in aqueous DMF (buffered at pH 7 by
HEFES), ionic strength = 0.01 M, at 25 C. For GSH and Hcys, change in absorbance at 275 nm was monitored. For Ala, Asn, Gln, Ser and Val,
change in absorbance at 295 nm was monitored. For Asp, His, Glu, Gly, Leu, Lys, Met, Phe and Pro, change in absorbance at 325 nm was
monitored. For Arg, change in absorbance at 395 nm was monitored.
2
R = 0.996
-6
-8
2
R = 0.994
-6
-4
-4
-4
-2
-2
-2
0
0
0
500
1000
1500
2000
2500
3000
0
0
3500
1000
2000
3000
0
1000
1/[Phe]
1/[Lys]
-160
-14
-140
-12
-120
2000
3000
1/[Pro]
-30
-25
-10
-20
2
R = 0.999
-60
-8
AO/(A - AO)
-80
AO/(A - AO)
AO/(A - AO)
-100
2
R = 0.999
-6
2
R = 0.993
-15
-10
-4
-40
-5
-2
-20
Figure S9 – Spectroscopic titration of Pt(DMSO)2Cl2 (2  10-5 M) with common amino acids and GSH in aqueous DMF (buffered at pH 7 by
1/[Ala] Asn, Gln, Ser and Val,
HEFES), ionic strength 1/[Ser]
= 0.01 M, at 25 C. For GSH and Hcys, change 1/[Val]
in absorbance at 275 nm was monitored. For Ala,
0
0
0
1000
2000
3000
4000
0
0
1000
2000
3000
0
1000
2000
3000
4000
5000
6000
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
change in absorbance at 295 nm was monitored. For Asp, His, Glu, Gly, Leu, Lys, Met, Phe and Pro, change in absorbance at 325 nm was
monitored. For Arg, change in absorbance at 395 nm was monitored.
-25
-2.0
-16
-1.8
-14
-20
-1.6
-12
-1.4
2
R = 0.999
-0.8
AO/(A - AO)
-1.0
AO/(A - AO)
AO/(A - AO)
-10
-15
-1.2
2
R = 0.993
-10
2
R = 0.990
-8
-6
-0.6
-4
-5
-0.4
-2
-0.2
0
0.0
0
100
200
300
400
500
600
700
800
900
0
0
1000
1000
2000
3000
4000
0
1000
1/[Asn]
1/[Arg]
-14
-25
2000
3000
1/[Asp]
-30
-12
-25
-20
-10
-20
2
-10
-8
AO/(A - AO)
R = 0.993
AO/(A - AO)
AO/(A - AO)
-15
2
R = 0.999
-6
-15
2
R = 0.998
-10
-4
-5
-5
-2
0
0
0
1000
2000
3000
1/[Gln]
4000
5000
6000
0
0
1000
2000
1/[Glu]
3000
0
1000
2000
3000
1/[Gly]
4000
5000
6000
Supplementary Material for Dalton Transactions
This journal is © The Royal Society of Chemistry 2004
Table S1 – Comparison of the energy of formation of adducts between various amino acids, GSH, cis-[RuII(bpy)2(CN)2] and
K2RuII(tBubpy)(CN)4 and different acceptor metal centers.
cis-Ru(bpy)2(CN)2 K2Ru(tBubpy)(CN)4
GSH
Cys
Hcys
Met
His
Ser
Asp
Glu
Arg
Gly
Ala
Val
Leu
Asn
Gln
Lys
Phe
Pro
No ref.
44.5(b)
No ref.
49.6(b)
75.3(b)
71.3(b)
45.6(b)
51.3(b)
50.8(b)
47.4(d)
50.8(b)
43.9(b)
No ref.
46.2(b)
No ref.
No ref.
(b)
(b)
(b)
(b)
(b)
(b)
(b)
(b)
(b)
(b)
(b)
(b)
(b)
15.4(b)
CrCl3·6H2O
11.8(a)
18.3(a)
No ref.
50.2(b)
MnCl2·4H2O
17.2
(a)
(a)
(b)
(b)
No ref.
29.1
FeCl2·4H2O
16.1(a)
18.9(a)
18.0(a)
18.0(a)
18.7(a)
7.8(a)
15.3(a)
14.5(a)
7.7(a)
14.3(a)
10.1(a)
12.1(a)
5.4(a)
11.2(a)
u.d.
14.2(a)
11.5(a)
7.4(a)
10.6(a)
7.7(a)
CoCl2·6H2O
8.2(a)
27.0(a)
29.1(b)
49.6(b)
No ref.
25.1(b)
40.5(b)
26.8(b)
35.9(b)
28.5(b)
24.5(b)
28.5(b)
26.2(b)
26.2(b)
25.7(b)
26.2(b)
24.5(b)
29.1(b)
24.0(b)
30.2(b)
NiCl2·6H2O
10.6(a)
23.1(a)
33.7(b)
53.6(b)
No ref.
31.9(b)
50.7(b)
30.8(b)
43.9(b)
38.2(b)
29.1(b)
34.2(b)
32.5(b)
31.4(b)
31.9(b)
33.7(b)
30.8(b)
34.8b)
30.2(b)
34.8(b)
CuCl2·2H2O
18.5(a)
29.4(a)
No ref.
39.9(b)
No ref.
46.2(b)
59.3(b)
46.8(b)
51.3(b)
48.5(b)
45.1(b)
48.5(b)
47.9(b)
46.8(b)
48.5(b)
45.6(b)
43.9(b)
47.9(b)
46.8(b)
51.9(b)
ZnCl2
11.7(a)
27.0(a)
52.5(b)
54.2(b)
No ref.
26.2(b)
38.8(b)
27.4(b)
35.9(b)
35.4(b)
24.5(b)
30.2(b)
28.0(b)
26.8(b)
28.0(b)
26.8(b)
26.2(b)
38.2(b)
28.0(b)
31.4(b)
Pd(DMSO)2Cl2
26.0(a)
31.1(a)
No ref.
155.7(b)
No ref.
95.8(b)
84.1(b)
62.8(b)
59.3(b)
59.3(b)
No ref.
62.8(b)
65.0 (b)
65.0 (b)
65.0 (b)
73.0(b)
62.8(b)
65.6(b)
62.2(b)
66.2(b)
Pt(DMSO)2Cl2
24.6(a)
31.4(a)
27.7(a)
27.4(a)
27.4(a)
25.8(a)
14.4(a)
5.8(a)
14.4(a)
12.9(a)
3.9(a)
11.7(a)
12.8(a)
13.8(a)
9.9(a)
12.6(a)
14.9(a)
12.2(a)
9.6(a)
11.6(a)
21.5
20.5
28.5
21.7
15.4
22.8
20.0
16.0
17.7
16.5
16.0
18.3
17.7
Note: a Go were measured by spectroscopic titration in DMF: phosphate pH 7 aqueous buffer (v/v 1:1), ionic strength 0.01M at 25°C (Figure S9).
b
Go cited from SC-Database. Data were obtained at 25°C in aqueous media.
n.d. – too small to be determined
18.3
(b)
12.6
18.3