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. Author manuscript; available in PMC: 2017 Jun 21.
Published in final edited form as: Biochemistry. 2016 Apr 4;55(15):2197–2213. doi: 10.1021/acs.biochem.5b01354

Table 2.

Octet Biolayer Interferometry Binding Parametersa for gp120–Antibody Interactions with CD4i-Binding Antibodiesb

antibody parameter FL ΔV3 ΔV1/V2 Coree
 17b ka (M−1 s−1) 2.5(1) × 104 8.1(5) × 104 6(1) × 105 1.34(5) × 106
kd (s−1) 8(1) × 10−5 1.4(2) × 10−4 9.7(2) × 10−5 3.5(9) × 10−5
KD (nM) 3.0(3) 1.73(8) 1.6(3) × 10−1 2.6(8) × 10−2
 48d ka (M−1 s−1) 4.8(4) × 104 8.9(1) × 104 6.6(5) × 105 1.6(1) × 106
kd (s−1) 1.54(1) × 10−4 8.9(3) × 10−5 1.5(5) × 10−4 3.8(3) × 10−4
KD (nM) 3.2(3) 1.01(5) 2.4(9) × 10−1 2.42(7) × 10−1
 A32 ka (M−1 s−1) 1.12(1) × 105 2.69(8) × 105 6.4(2) × 105 8.220(3) × 105
kd (s−1) 1.72(6) × 10−5 7.04(3) × 10−5 4.8(3) × 10−5 4(1) × 10−5
KD (nM) 1.54(5) × 10−1 2.62(7) × 10−1 7.5(7) × 10−2 4.1(9) × 10−2
 N5i5 ka (M−1 s−1) 7.7(4) × 104 1.97(9) × 105 6.4(6) × 105 1.11(3) × 106
kd (s−1) ndc ndc ndc ndc
KD (nM) ndc ndc ndc ndc
a

ka, rate of association; kd, rate of dissociation; KD, equilibrium dissociation constant.

b

Values are means ± standard deviations. Standard errors are for two independent measurements, presented in parentheses with respect to the smallest number place value: 2.4(1) × 104 is equivalent to 24000 ± 1000.

c

Because of slow dissociation, dissociation rates or binding constants could not be reliably fit.