. 2019 Dec 2;9:18143. doi: 10.1038/s41598-019-54211-0

Table 3.

Results of the ITC measurements for VEGF₁₆₅-HBD and psHA dp4.

compound	c^a_protein	c^a_ligand	N^b	ΔG^c	ΔH^d	TΔS^e	K_D^f	$\bar{x}$ (K_D)^g
psHA dp4^h	15	60	0.505	−36.8	−17.3	+19.5	357 ± 21	378 ± 21
psHA dp4^h	15	60	0.481	−36.5	−17.1	+19.4	398 ± 10	378 ± 21
psHA dp4ⁱ	15	60	0.523	−36.4	−3.7	+32.7	431 ± 245	364 ± 48
			0.557	−37.0	−7.2	+29.7	341 ± 73
			0.429	−37.1	−4.6	+32.5	320 ± 200
psHA dp6ⁱ	15	50	0.628	−39.0	−4.8	+34.2	149 ± 80	124 ± 29
			0.409	−40.5	−5.7	+34.8	83 ± 30
			0.599	−39.2	−5.0	+34.2	140 ± 65

^aConcentration in µM, ^bmolar binding ratio of the ligand-protein interaction (stoichiometry), ^cbinding free energy in kJ∙mol⁻¹, ^dbinding enthalpy in kJ∙mol⁻¹, ^dentropic contribution term in kJ∙mol⁻¹, ^fdissociation constant in nM, ^gmean of the calculated K_D values, ^hITC measurements were performed in 8 mM phosphate buffer with 2 mM NaCl, ⁱITC measurement were performed in 10 mM PBS buffer with 140 mM NaCl.