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1.4 1.2 1 Absorbance (a.u.) 0.8 0.6 0.4 0.2 0 250 [C12E4]
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Wavelength (nm) 3 50 2.5 Abs/[azo] (DO.mM 1) 40 2 30 1.5 20
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0 0 0.2 0.4 0.6 [TX 100] g/L (b) 0.8 1
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Figure 7.6. Indices of association of azobenzene onto hydrophobic domains. (a) Representative spectra of an azo-modi ed polymer in water (under blue exposure) with increasing concentration of surfactant C12E4 (0 0.4 g/L). Polymer structure: cf. left-hand side in Fig. 7.1, with n = 11 and x = 2%. (b) Variation of the fraction of bound azobenzene upon addition of Triton X 100 in a solution of polymer at xed concentration (polymer similar as in (a), with n = 5 and x = 4%).
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electrostatic repulsion that opposes a strong penalty to the formation of loops shorter or closer than the Debye length. Exposure to UV irradiation triggers the detachment of the bound micelles (or proteins) (Pouliquen and Tribet, 2006; Pouliquen et al., 2002). Likewise, we cannot detect signi cant sensitivity to the presence of nanoparticles of the absorption spectrum of the predominantly cis polymer (not shown). However, to obtain more accurate determinations of the degree of light-triggered release, the average number of bound micelles (or protein) per chain was measured. Chromatographic methods under continuous injection mode, in this case, capillary electrophoresis, enable one to separate minute amount of free particles with no marked perturbation of the binding equilibrium [the method is also called frontal analysis; see Gao et al. 1997] Representative binding isotherms in Fig. 7.7 obviously point to UV-triggered releases. The degree of photodissociation depends, however, on the composition of the complexes. In the case of the protein bovine serum albumin, we measured an increasing degree of dissociation with the decreasing number of protein per chain (Fig. 7.7b and Pouliquen and Tribet, 2006). Saturated chains with typically one bound protein per one to three azobenzene groups do not respond to light, which points to the lack of speci city of the protein toward the isomerization state of the azobenzene. Nevertheless, chains with less than 2 4 g/g of bound protein (i.e., less than three proteins per 1000 monomers and 10 30 azobenzene groups per bound protein) release up to 90% of their protein content upon exposure to blue light. In contrast, surfactants such as Triton X100 (Fig. 7.7a) and C12E4 (Khoukh et al., 2007) do not photodissociate at low degree of loading of the micelles in the chains (close to the critical micellar concentration, where B20 40 azobenzene bind to 100 surfactants). The photoresponse increases regularly with increase in the loading of surfactant and accordingly decrease in the amount of bound azo per micelle. A tentative interpretation is proposed that in both cases, an optimal number of ca. 10 20 bound azobenzene per bound nanoparticle must be reached for optimal responses to be reached. The following arguments present the basic reasons for an optimal azo/particle ratio, and the expected polymer-related ampli cation of af nity. Binding of an isolated azobenzene on a single nanoparticle should a priori be described by using a conventional equilibrium constant as for 1:1 complexation (we will call this incipient binding the Benessi Hildebrand regime). Once the rst link onto a micelle (or a protein) is formed, the loss of conformation entropy for loop formation represents the primary penalty for further associations of azobenzenes. Accordingly, the free energy gain for transferring the azobenzene in its binding site (hydrophobic association) must be reduced by a term of the order of Floop=kT Ln N [with N being the length between successive chromophores in the chain; Lairez et al. (1997)]. Obviously, short loops should be preferred to long ones. This point retains its validity even when interloop repulsions are taken into account and if a large number of azo can bind to the same particle (Borisov and Halperin, 1995). Consequently, it is expected that the association abruptly changes from a Benessi Hildebrand regime to multisite and correspondingly tight association if the loop penalty becomes
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