Table 1.
Introduction of disulfide bonds and engineering of non-covalent interactions in CH2 and CH3 domains.
| Position | Domaina | ΔTm (°C) | Descriptionb | Reference |
|---|---|---|---|---|
| Covalent | ||||
| L242C/K334C | CH2 | 18.7 | Isolated IgG1 CH2 | (55) |
| V240C/L334C | CH2 | 11.2 | Isolated IgG1 CH2 | (55) |
| L242C/K334C | CH2 | 8.7 | CH2 in IgG1 | (79) |
| L242C/K334C | CH2 | 2.1 | CH2 in aglycosylated IgG1 | (81) |
| A287C/L306C | CH2 | 7.8 | CH2 in aglycosylated IgG1 | (81) |
| R292C/V302C | CH2 | 8.1 | CH2 in aglycosylated IgG1 | (81) |
| P343C/A431C | CH3 | 35.4 | Isolated IgG1 CH3 | (82) |
| P343C/A431C | CH3 | 10.2 | CH3 in IgG1 Fc | (83) |
| S375C/P396C | CH3 | 4.7 | CH3 in IgG1 Fc | (83) |
| P343C/A431C | CH3 | 15.2 | CH3 in IgG1 Fc | (83) |
| S375C/P396C | ||||
| P445G/G446E/K447C | CH3 | 3.5 | CH2 in IgG1Fc | (84) |
| 9.1 | CH3 in IgG1 Fc | (84) | ||
| P343C/A431C | CH3 | 14.5 | CH2 in IgG1 Fc | (84) |
| P445G/G446E/K447C | 18.1 | CH3 in IgG1 Fc | (84) | |
| Non-covalent | ||||
| L235K/L309K | CH2 | 2.7 | CH2 in IgG | (45) |
| L234F/L235Q K322Q/M252Y S254T/T256E | CH2 | 5.7 | Compare to IgG1 with Mutation of “TM-YTE” | (99) |
| G197K/S207G/T246L | Bovine CH3 | 10.0 | Compare to bovine wtCH3 | (102) |
| Q295F/Y296A | CH2 | 3.2 | CH2 in IgG1 Fc | (103) |
| Truncation of N-terminal residues “APELLGG” | CH2 | 5.1 | Isolated IgG1 CH2 | (107) |
aAll the domains are from human IgG1 if not specified.
bAll the islolated domains are expressed in Escherichia coli, others are expressed in eukaryotic cells.