Table 2 Best-fit binding parameters from GMMA of static and dynamic light scattering and sedimentation velocity.

From: Global multi-method analysis of interaction parameters for reversibly self-associating macromolecules at high concentrations

mAb

Model

s1(a) (S)

kS,SV(b) (mL/g)

KD,glob

B2,glob (mL/g)

kD,glob (mL/g)

Irrev. dimer(c) (wt%)

Irrev. aggreg.(d) (wt%)

B

1

6.73

6.5 (0.2)

∞ (> 17 mM)

1.13 (0.12)

 − 4.24

5.7

0.06 (< 0.01)

A

1–2

6.67

5.0 (0.3)

7.1 mM (5.9–8.5)

 − 2.13 (0.11)

 − 9.26

1.8

0.07 (< 0.01)

E

1–2

6.70

0.2 (< 0.01)

550 µM (510–730)

 − 7.7 (0.2)

 − 15.6

0.1

0.01 (< 0.01)

D

1–2 and 2–4…isoH

6.72

3.5 (0.2)

153 µM (136–169) and 5.3 mM (2.7– 75)

0.01 (0.23)

 − 3.5

6.4

0.02 (0.03)

C

1–2 and 2–4

6.41 (0.16)

3.6 (2.2)

15 µM (14.7–21) and 48 µM (40–51)

 − 5.9 (0.68)

 − 15.4

0.4

0.0 (< 0.01)

  1. Values in parentheses are confidence intervals or +/− errors, respectively, on a confidence level of 68.3%.
  2. (a)The monomer s-value was determined from the c(s) analysis of sedimentation under ideal conditions at 0.3 mg/mL and fixed in the analysis, except for mAb C.
  3. (b)Nonideal cNI(s0) analysis was carried out to pre-determine kS24.
  4. (c)Irreversible dimer with assigned f/f0 = 1.8, at pre-determined population from SV in dilute solution, except for mAb E where best-fit parameters are shown.
  5. (d)As a representation of very large trace aggregates, weight-percent of non-interacting species of 10 MDa with f/f0 = 1.8.
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