Douhal et al. 10.1073/pnas.0507459102.

Supporting Information

Files in this Data Supplement:

Supporting Text
Supporting Figure 8
Supporting Figure 9
Supporting Table 1
Supporting Table 2
Supporting Figure 10




Supporting Figure 8

Fig. 8. The change in the UV-visible absorption spectra of orange II (OII) in water (buffer, pH 7) upon addition of human serum albumin (HSA) protein is shown. (A) Change in UV-visible absorption spectra of OII in buffer (pH » 7) upon addition of HSA protein. (B) Variation of the absorption intensity difference (A0 – A) at 485 nm with the added HSA concentration. The solid line is the fit of the experimental data supposing 1:1 complex and adopting the model in ref. 1.

1. Bourson, J., Pouget, J. & Valeur, B. (1993) J. Phys. Chem. 97, 4552–4557.





Supporting Figure 9

Fig. 9. Magic-angle emission decays of OII in water and in the presence of 15 mM b-cyclodextrin (CD) and g-CD, and of 20 mM HSA protein. The excitation and observation wavelengths were 393 and 620 nm, respectively. The solid curves are from the best fits giving times posted in Table 1.





Supporting Figure 10

Fig. 10. Anisotropy decay (620 nm) of OII in presence of 20 mM HSA. The solid line is from the best fit giving time constant of 630 (± 50) ps.





Table 1. Time constants and normalized (to 1) amplitudes from the multiexponential fits of the ps-emission decays of OII in water and in the presence of 15 mM β- and g-CD and of 20 μM HSA protein

Medium

Wavelength, nm

t1, ps a1

t2, ps a2

t3, ns a3

Water

560–630

12 100

–

–

b-CD

560

25 89

150 10

0.9 1

630

45 66

175 34

0.7 1

g-CD

560

25 91

135 8

0.6 1

630

35 79

155 18

0.7 3

HSA

560

35 91

185 9

–

630

45 88

205 12

–

The observation wavelengths are indicated.





Table 2. Time constants and normalized (to 1) amplitudes from the multiexponential fits of the fs-emission transients of OII in the used media

Medium; lobs, nm

t1, fs a1

t2, ps a2

t3, ps a3

Water; 530

35 84

0.8 16

 

Water; 620

40 80

0.9 14

4.4 6

THF; 530

40 86

0.9 14

 

THF; 620

35 81

1.0 17

4.1 2

DMSO; 530

50 77

1.0 13

2.5 10

DMSO; 620

40 72

0.9 15

2.5 13

Triacetin; 530

40 84

1.1 13

7.5 3

Triacetin; 620

40 61

1.6 36

4.5 3

EG; 530

35 79

1.2 13

4.7 8

EG; 620

30 67

1.1 20

5.6 13

b-CD; 530

50 88

1.6 11

15* 2

b-CD; 620

85 63

2.5 25

45* 13

g-CD; 530

45 87

1.9 10

15* 3

g-CD; 620

85 62

2.4 25

35* 13

HSA; 530

40 79

1.7 10

15* 11

HSA; 620

85 66

2.6 20

45* 14

The observation wavelengths are indicated. THF, tetrahydrofuran; EG, ethylene glycol.

*A fixed value of this time in the fit.





Supporting Text

Experimental Part

For the femtosecond (fs) experiment, the polarization of the pump (390 nm) was set at the magic angle with respect to that of gating pulse (780 nm). The resulting up-converted signal was filtered and entered to a double monochromator for detection with a photomultiplier tube. The cross-correlation of the apparatus measured by gating the Raman signal from solvent is »170 fs. For both picosecond (ps) and fs experiments, the data were deconvoluted with the instrument response function of each apparatus, using dispersed light for the ps one and the cross-correlation function for the up-conversion apparatus, and fitted to a multiexponential function using the Fluofit package (Picoquant, Berlin). The quality of the fits was characterized in terms of residual distribution and reduced c2 value.