Table 7. Thermodynamic parameters and binding data for the interaction of FucC6 and Le^a glycopeptide dendrimers with LecB ^a .

Ligand	n Fuc	n b	ΔH [kcal mol–1]	–TΔS [kcal mol–1]	ΔG [kcal mol–1]	K D[nM]	r.p./nsugar
FucOCH3	1	0.77 ± 0.03	–9.87 ± 0.24	1.17 ± 0.24	–8.70 ± 0.02	430 ± 10	1
Lea	1	1.08 ± 0.01	–8.35 ± 0.02	–0.74 ± 0.002	–9.10 ± 0.02	213 ± 2.0	2
FucC6G2	4	0.22 ± 0.01	–14.7 ± 0.38	5.20 ± 0.28	–9.44 ± 0.09	121 ± 20	0.9 c
LeaC6G2	4	0.12 ± 0.01	–58.5 ± 1.17	48.5 ± 1.65	–10.1 ± 0.06	39 ± 0.8	2.8 c

^aThermodynamic parameters and dissociation constants K_D are reported as an average of two independent runs from ITC in 20 mM Tris, 100 mM NaCl, 100 μM CaCl₂, pH = 7.5. Isothermal Titration Calorimetry (ITC) data are for LecB binding. Titration concentrations for Ligand/LecB are indicated in brackets: Le^a (0.324 mM/0.0327), FucC₆G2 (0.3 mM/0.08 mM), Le^aC₆G2 (0.07 mM/0.042 mM).

^b n defined the stoichiometry of the binding.

^cRelative potency per fucoside. r.p./n_Fuc = K_D(FucOCH₃)/K_D(ligand)/n_Fuc. See ESI Fig. S107 for ITC plots.