Cargando…
Human IgG1 Fc pH-dependent optimization from a constant pH molecular dynamics simulation analysis
The binding of IgG Fc with FcRn enables the long circulating half-life of IgG, where the Fc–FcRn complex interacts in a pH-dependent manner. This complex shows stronger interaction at pH ≤ 6.5 and weaker interaction at pH ≥ 7.4. The Fc–FcRn binding mechanism that promotes the long circulating half-l...
Autores principales: | Lim, Yee Ying, Lim, Theam Soon, Choong, Yee Siew |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9051383/ https://www.ncbi.nlm.nih.gov/pubmed/35492131 http://dx.doi.org/10.1039/c9ra10712f |
Ejemplares similares
-
Construction of pH-sensitive Her2-binding IgG1-Fc by directed evolution
por: Traxlmayr, Michael W, et al.
Publicado: (2014) -
FcγRI FG-loop functions as a pH sensitive switch for IgG binding and release
por: Lu, Jinghua, et al.
Publicado: (2023) -
Effect of pH on the influenza fusion peptide properties unveiled by constant-pH molecular dynamics simulations combined with experiment
por: Lousa, Diana, et al.
Publicado: (2020) -
Best Practices
in Constant pH MD Simulations: Accuracy
and Sampling
por: Buslaev, Pavel, et al.
Publicado: (2022) -
Galvani Offset
Potential and Constant-pH Simulations
of Membrane Proteins
por: Bignucolo, Olivier, et al.
Publicado: (2022)