Skip to main content
. Author manuscript; available in PMC: 2013 Jul 16.
Published in final edited form as: Chembiochem. 2011 Dec 23;13(2):259–270. doi: 10.1002/cbic.201100638

Table 3.

Dissociation constants of type II homoarginine-equivalent arginine mimetic peptides (hAMII).

Kd,
μM		 Error ΔG,
kcal mol−1 		ΔΔGaffinity,
kcal mol−1 		ΔΔGspecificity,b
kcal mol−1
Src Arg 37 2 −6.0 0 +0.7
Dap-Ac 350 31 −4.7 1.33 −0.2
hArg(gGly) 59 2.3 −5.8 0.28 −0.6
hArg(gl-Val) 67 2.3 −5.7 0.35 −0.7
hArg(gd-Val) 130 3.7 −5.3 0.74 −0.4
hArg(gl-Phe) 58 1.8 −5.8 0.27 −0.5
hArg(gd-Phe) 66 2.1 −5.7 0.34 −0.9
hArg(gl-Trp) 24 1.2 −6.3 −0.26 −1.0
hArg(gd-Trp) 49 2.1 −5.9 0.17 −1.0
Grb Arg 12 0.7 −6.7 0
Dap-Ac 500 160 −4.5 2.20
hArg(gGly) 166 12 −5.1 1.56
hArg(gl-Val) 227 13 −4.9 1.74
hArg(gd-Val) 270 31 −4.9 1.84
hArg(gl-Phe) 128 8 −5.3 1.40
hArg(gd-Phe) 319 44 −4.8 1.94
hArg(gl-Trp) 121 10 −5.3 1.36
hArg(gd-Trp) 244 24 −4.9 1.78
a

ΔΔGaffinity = ΔG (peptide) – ΔG (Arg).

b

ΔΔGspecificity = ΔGSrc – ΔGGrb for a given peptide. All peptides except hAMII(Arg) (Kd = 102 ± 7 μM, ΔGCrk = −5.4 kcal mol−1), hAMII(gl-Trp) (Kd = 153 ± 9 μM, ΔGCrk = −5.2 kcal mol−1), and hAMII(gd-Trp) (Kd = 183 ± 11 μM, ΔGCrk = −5.1 kcal mol−1) bound poorly to Crk (Kd > 250 μM). All experiments were conducted in PBS at 25 °C.