TABLE 3.

Dissociation constants of the compounds studied in this work for HSA retrieved from the variation in the steady-state fluorescence intensity (K _d), from the variation in the fluorescence intensity corrected regarding the variation in fluorescence lifetime (K′ _d) and from the variation in $\overline{\tau }$ (K″ _d). The reverse of the constants computed from the slope in the Stern Volmer plot of fluorescence intensities corrected regarding the variation in fluorescence lifetime are also presented (1/K), as well as the dissociation constants of the compounds for the warfarin binding site in the presence of equimolar proportions of HSA and this competitor (K _dc). Octanol-water partition coefficients (log P _o/w). are also shown. All values result from the average of at least 3 independent experiments and are presented with the respective standard deviations (SD). Statistical significance versus INH: **, p < 0.01.

Compound	103 (K d ± SD)/M	103 (K′ d ± SD)/M	103 (1/(K ± SD))/M	103 (K′′ d ± SD)/M	103 (K dc ± SD)/M	log P o/w ± SD
INH	2.72 ± 0.04	2.72 ± 0.04	1.65 ± 0.06	-	4.55 ± 0.05	−0.85 ± 0.01 b
INH-C10	0.046 ± 0.009**	0.05 ± 0.02**	0.07 ± 0.01**	0.120 ± 0.003	0.4 ± 0.2**	3.5 ± 0.2 b
N33	0.16 ± 0.05**	0.2 ± 0.1**	0.12 ± 0.04**	0.08 ± 0.06	0.054 ± 0.004**	1.32 ± 0.06 c
N34	0.13 ± 0.05**	0.11 ± 0.05**	0.07 ± 0.03**	0.52 ± 0.02 a	0.128 ± 0.005**	3.7 ± 0.1 c
N33red	0.6 ± 0.2**	0.6 ± 0.2**	0.56 ± 0.05**	-	0.9 ± 0.3**	1.33 ± 0.04
N34red	0.15 ± 0.03**	0.14 ± 0.04**	0.090 ± 0.001**	0.73 ± 0.06 a	0.34 ± 0.02**	2.6 ± 0.2

^aK values correspond to the slopes obtained from the Stern Volmer plot using the amplitude-weighted mean fluorescence lifetimes.

^bRetrieved from reference (Ràfols et al., 2012).

^cRetrieved from reference (Martins et al., 2014).