Does aggregation modulate the apparent association constant of host–guest complexes and related species?

1997 ◽  
Vol 93 (12) ◽  
pp. 2153-2160 ◽  
Author(s):  
Bertrand Hamelin ◽  
Ludovic Jullien
2015 ◽  
Vol 11 ◽  
pp. 514-523 ◽  
Author(s):  
Lars W Städe ◽  
Thorbjørn T Nielsen ◽  
Laurent Duroux ◽  
Reinhard Wimmer ◽  
Kyoko Shimizu ◽  
...  

A novel β-cyclodextrin (β-CD) dimer was synthesized and surface-grafted by click chemistry onto azide-functionalized quartz surfaces in order to introduce the cooperative features of the β-CD dimer to solid surfaces. Using NMR and fluorescence spectroscopy, it is shown that the free β-CD dimer forms a 1:1 complex with the fluorescent guest molecule, 2-anilinonaphthalene-6-sulfonic acid (otherwise known not to form 1:2 complexes with parent β-CD), with an apparent association constant of 7300 M−1. Further, it is shown using total internal reflection fluorescence spectroscopy that the inclusion of the fluorescent guest into both cavities of the β-CD dimer is maintained when grafted onto a solid surface.


1973 ◽  
Vol 57 (2) ◽  
pp. 289-298 ◽  
Author(s):  
A. F. CLARK ◽  
C. E. BIRD

SUMMARY The binding of 5α-androstane-3α,17β-diol to human plasma proteins was studied by equilibrium dialysis. The mean value of 96·6% for men was significantly less than that of 97·5% for women. These values are higher than those found for 5α-dihydrotestosterone (95·0 and 97·3%, respectively) and for testosterone (92·4 and 95·3%, respectively). When the distribution of labelled steroid in the different protein fractions was studied by paper electrophoresis, male plasma showed a larger fraction of 5α-androstane-3α,17β-diol radioactivity in the albumin fraction and less in the β-globulin area than did female plasma. Similar finding were made when 5α-dihydrotestosterone was studied. No inter-α-globulin peak of radioactivity was found for 5α-androstane-3α,17β-diol and 5α-dihydrotestosterone as occurs for testosterone. Albumin binds more 5α-androstane-3α,17β-diol than 5α-dihydrotestosterone or testosterone when studied by equilibrium dialysis and this is due to a higher apparent association constant between albumin and the dihydroxysteroid.


2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
N. Nagarajan ◽  
G. Paramaguru ◽  
G. Vanitha ◽  
R. Renganathan

The photochemical behavior of xanthene dyes (fluorescein, erythrosine, and eosin) with colloidal SnO2nanoparticles was probed by UV-visible, steady state, and time resolved fluorescence measurements. The prepared SnO2nanoparticles were characterized by using UV-visible and powder XRD measurements. The xanthene dyes were adsorbed on the surface of colloidal SnO2nanoparticles through electrostatic interaction. Apparent association constant (Kapp) was calculated from the relevant fluorescence data. The larger value of apparent association constant indicates a strong association between xanthene dyes and SnO2nanoparticles. The fluorescence quenching is mainly attributed to electron transfer from the excited state xanthenes to the conduction band of colloidal SnO2. The electron transfer mechanism was explained based on the Rehm-Weller equation as well as the energy level diagram.


1976 ◽  
Vol 159 (3) ◽  
pp. 627-631 ◽  
Author(s):  
M S Wooster ◽  
J M Wrigglesworth

1. The adsorption of [14C]carboxymethylated glyceraldehyde 3-phosphate dehydrogenase to negatively charged liposomes of phsphatidic acid/phosphatidylcholine (3:7, w/w) was investigated. The apparent association constant at I/2 = 60, pH 7.6, was 0.4 × 10(6)M-1. Adsorption decreased as ionic strength and pH were increased. 2. In the presence of negatively charged liposomes, the Km value for glyceraldehyde 3-phosphate of glyceraldehyde 3-phosphate dehydrogenase was increased and Vmax. decreased. In the presence of positively charged liposomes, the Km value for glyceraldehyde 3-phosphate decreased and there was no significant change in Vmax. Addition of Triton X-100 abolished the effect of both positively and negatively charged liposomes on the kinetic properties of the enzyme.


1978 ◽  
Vol 88 (1) ◽  
pp. 29-37 ◽  
Author(s):  
B. Koch ◽  
B. Lutz-Bucher ◽  
B. Briaud ◽  
C. Mialhe

ABSTRACT The aim of this study was to determine whether pituitary glucocorticoid binding sites are under hormonal control. It was shown that corticosterone and thyroxine exerted antagonistic effects on both the transcortin-like component and true receptor present in the hypophysis: thyroid hormones, in contrast to glucocorticoids which exhibited opposite influence, increased maximum binding without affecting significantly the apparent association constant. Thus, it seems that the concentration of glucocorticoid binding sites is regulated by the glucocorticoid ligands, as well as by a different hormone. Moreover, a striking parallelism was found between plasma transcortin and pituitary transcortin-like capacity, argueing in favour of a plasma origin for this pituitary binder.


1987 ◽  
Vol 42 (8) ◽  
pp. 849-852
Author(s):  
P. Becker ◽  
B. A. Bilal

The association constant of acetic acid in 1.02 m (NaCl) aqueous solution has been determined potentiometrically at temperatures up to 260 °C and pressures up to 1005 bar. A high-temperature high-pressure concentration cell having two hydrogen electrodes has been used for the measurement. The apparent association constant Q′HAC increases with increasing temperature but decreases with increasing pressure: (Q′HAC)25 ° C, 108 bar = 2.86 · 104, (Q′HAC)25 ° C , 500bar = 2.7 · 104, (Q′HAC)200 °C, 500 bar = 4.65 · 104, (Q′HAC)26O °C, 1005 bar = 6.57 · 104 m−1.


1985 ◽  
Vol 232 (3) ◽  
pp. 663-667 ◽  
Author(s):  
B D Wilson ◽  
W L Gent

K'A (apparent association constant) and Bmax. (total receptor concentration) describing the interaction of tri-iodothyronine (T3) and its solubilized rat liver nuclear receptor (R) are found to be moderately consistent in successive preparations, but both quantities diminished after a few days. To achieve comparability in the effects of ionic strength (I) and of pH on K'A and Bmax, appropriate measurements have been made simultaneously on single preparations. K'A and Bmax. were found to be effectively unchanged over the range I0.05-0.60. Both parameters have been measured over the range pH 6.4-9.0 and the values of K'A analysed in terms of the 4′-OH ionization of T3 and that of a cationic acidic group, shown to require pK' = 7.6. This group could be identified either with the terminal alpha-NH3+ of T3 or with a group (RH+) in the receptor site. On the balance of evidence the first possibility is the more likely, in which case the variation of Bmax. with pH is ascribed to conformational changes in the receptor protein.


1978 ◽  
Vol 78 (2) ◽  
pp. 171-177 ◽  
Author(s):  
B. Y. TANG ◽  
N. R. ADAMS

SUMMARY The binding of [3H]oestradiol-17β to the hypothalamus and pituitary gland of cloveraffected permanently infertile and control ovariectomized ewes was compared in vivo and in vitro. When [3H]oestradiol-17β was infused into the carotid artery (10 ng/min), the total homogenate and the nuclear and protamine-precipitable cytosol fractions of hypothalami and pituitary glands from clover-affected ewes bound significantly more [3H]oestradiol than those of the controls. Cytoplasmic oestradiol-17β receptors from the pituitary glands of clover-affected ewes showed a significantly lower apparent association constant and a higher number of binding sites/mg protein in vitro. It is suggested that the hypothalami and pituitary glands of ewes made permanently infertile by oestrogenic clover are less sensitive to feedback regulation of oestradiol-17β at physiological levels.


1989 ◽  
Vol 256 (6) ◽  
pp. C1250-C1256 ◽  
Author(s):  
S. M. Harrison ◽  
D. M. Bers

The association constants of ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) for protons and Ca can be used to calculate the apparent association constant of EGTA for Ca (K'CaEGTA). This value is often used in calculating the free [Ca2+] of complex solutions such as those used to determine the Ca sensitivity of skinned muscle fibers. As association constants are usually measured at 0.1 M ionic strength and between 20 and 25 degrees C, these constants must first be adjusted for conditions different from those at which they were measured, before calculation of K'CaEGTA. The proton and Ca association constants (and their delta H values) from A. E. Martell and R. M. Smith (Critical Stability Constants, New York: Plenum, vol. 1, 1974) adjusted for ionic strength and temperature using a semiempirical Debye-Huckel formalism and Van't Hoff isochore, respectively, closely describe the influence of both ionic strength and temperature on K'CaEGTA. Errors in the adjustment or calculation of association constants can dramatically affect the calculated value of K'CaEGTA and hence the calculated free [Ca2+] of complex solutions, such as those used to mimic the intracellular environment.


1992 ◽  
Vol 86 (1) ◽  
pp. 168-172 ◽  
Author(s):  
Faustino Menegus ◽  
Liliana Cattaruzza ◽  
Leonardo Scaglioni ◽  
Enzio Ragg

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