Antibody Fc engineering for enhanced neonatal Fc receptor binding and prolonged circulation half-life
The neonatal Fc receptor (FcRn) promotes antibody recycling through rescue from normal lysosomal degradation. The binding interaction is pH-dependent with high affinity at low pH, but not under physiological pH conditions. Here, we combined rational design and saturation mutagenesis to generate nove...
Saved in:
Main Authors: | Brian C. Mackness (Author), Julie A. Jaworski (Author), Ekaterina Boudanova (Author), Anna Park (Author), Delphine Valente (Author), Christine Mauriac (Author), Olivier Pasquier (Author), Thorsten Schmidt (Author), Mostafa Kabiri (Author), Abdullah Kandira (Author), Katarina Radošević (Author), Huawei Qiu (Author) |
---|---|
Format: | Book |
Published: |
Taylor & Francis Group,
2019-10-01T00:00:00Z.
|
Subjects: | |
Online Access: | Connect to this object online. |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Pharmacokinetics of novel Fc-engineered monoclonal and multispecific antibodies in cynomolgus monkeys and humanized FcRn transgenic mouse models
by: Delphine Valente, et al.
Published: (2020) -
Engineered Fc-glycosylation switch to eliminate antibody effector function
by: Qun Zhou, et al.
Published: (2020) -
The influence of antibody engineering on Fc conformation and Fc receptor binding properties: Analysis of FcRn-binding engineered antibodies and an Fc fusion protein
by: Takuo Suzuki, et al.
Published: (2021) -
Systematic analysis of Fc mutations designed to reduce binding to Fc-gamma receptors
by: Geoff Hale, et al.
Published: (2024) -
Systematic analysis of Fc mutations designed to enhance binding to Fc-gamma receptors
by: Geoff Hale, et al.
Published: (2024)