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. 2009 Nov 11;84(2):1076–1088. doi: 10.1128/JVI.02113-09

TABLE 2.

Binding kinetics of interactions between anti-HIV antibody fragments to SF162-derived epitope peptidesa

Epitope KD (nM) SF162 gp140 monomer binding
SF162 gp140 trimer binding
kOFF/kON (nM) kON (M−1 s−1) kOFF (s−1) kOFF/kON (nM) kON (M−1 s−1) kOFF (s−1)
Fv4E10wt 12 (1) 108 (1) [2.50 (2)] E4 [2.70 (2)] E-3 98 (1) [2.70 (2)] E4 [2.60 (2)] E-3
Fv4E10[W(H100)A] 14 (1) 106 (2) [2.40 (2)] E4 [2.50 (2)] E-3 119 (2) [2.10 (2)] E4 [2.50 (2)] E-3
Fv4E10[G(L50)E] 16 (1) 136 (2) [2.00 (2)] E4 [2.70 (2)] E-3 114 (2) [2.00 (2)] E4 [2.30 (2)] E-3
Fab4E10 10 (1) 130 (2) [1.70 (2)] E4 [2.20 (2)] E-3 135 (2) [2.00 (2)] E4 [2.70 (1)] E-3
IgG447 199 (6)
Fab447 (state 1) 92 (2)* [3.40 (5)] E5 [4.90 (9)] E-2 93 (1)* [2.60 (2)] E5 [3.60 (3)] E-2
Fab447 (state 2) [2.06 (2)] E-3 [3.45 (4)] E-3 [2.66 (7)] E-3 [5.8 (1)] E-3
a

Values are means, with standard errors in parentheses. Epitope peptides were the 4E10 or 447-52D sequence or gp140 monomers or trimers as measured by SPR at 25°C. *, equilibrium constants were determined using BIAevaluation 2.0 software (Biacore AB) with a two-state fitting model; state 2 on-rates have units of s−1.