. Author manuscript; available in PMC: 2023 Jul 28.

Published in final edited form as: ACS Infect Dis. 2022 Jan 17;8(2):296–309. doi: 10.1021/acsinfecdis.1c00432

Table 1. Biophysical Data for Selected Fragments Showing the Change in Protein Melting Temperatures (ΔT_m), Binding Affinities (K_d), and Ligand Efficiencies (LE)^a.

Compound	ΔTm (°C)^b	MabPurC K_d (μM)	LE^d
1	+3.6	341 ± 14	0.53
2	ND	ND	_
3	+4.0	159 ± 9	0.52
4	+1.7^c	1060 ± 252	0.45
5	+1.0	971 ± 29	0.51
6	+2.5	442 ± 22	0.51
7	+1.7	ND	_
8	+0.7	ND	_

ND not determined.

5 mM ligand and 100 μM MabPurC.

3 mM ligand and 70 μM MabPurC.

kcal mol^–1 per heavy atom.

Table 1. Biophysical Data for Selected Fragments Showing the Change in Protein Melting Temperatures (ΔTm), Binding Affinities (Kd), and Ligand Efficiencies (LE)a.