2013年11月5日 · Using yeast display, we identified human serum albumin (HSA) variants with increased affinity for human FcRn at endosomal pH, enabling us to solve the crystal structure of a variant HSA/FcRn complex.

2018年10月2日 · In the current study, we aimed to investigate how differences in the amino acid composition of DI between MSA and HSA affect receptor binding. We found that targeting residues within the two DI...

2018年2月12日 · Here, we report on a novel human endothelial cell-based recycling assay (HERA) that can be used for such pre-clinical screening. In HERA, rescue from degradation depends on FcRn, and engineered...

针对与HSA和/或hFcRn结合化合物进行PK/PD研究，提高准确性及预测性； 各种化合物的PK差异性评估，包括白蛋白变体，小分子，抗体及抗体样生物制剂等，筛选最优化合物。

2013年11月5日 · The long circulating half-life of serum albumin, the most abundant protein in mammalian plasma, derives from pH-dependent endosomal salvage from degradation, mediated by the neonatal Fc receptor (FcRn). Using yeast display, we identified human serum albumin (HSA) variants with increased affinity for …

人血清白蛋白 (HSA) 通过新生儿 Fc 受体 (FcRn) 介导的再循环机制，由于其超长的血清半衰期，已被用于延长治疗性蛋白质的血清半衰期。 在大多数情况下，只有一种 HSA 分子与治疗性蛋白质结合，导致血清半衰期有限延长。

human serum albumin (HSA) variants with increased affinity for human FcRn at endosomal pH, enabling us to solve the crystal structure of a variant HSA/ FcRn complex. We find an extensive, primarily hydrophobic interface stabilized by hydrogen-bonding networks involving protonated histidines internal to each protein. The interface features two

2023年2月24日 · 为了延长体内半衰期，TrYbe®的一个靶标结合结构域被设计为人血清白蛋白 （HSA） 特异性，HSA延长半衰期的主要机制和FcRn介导的HSA回收有关。 TrYbe®分子另外一个尤为关键的特征是在scFv VH44-VL100引入的二硫键，这对于其结构稳定性尤为重要。

FcRn (neonatal Fc receptor for IgG)是由 FCGRT (Fc fragment of IgG receptor and transporter) 基因编码的α重链与胞外 β2-微球蛋白 （β2m）轻链非共价结合构成的异二聚体。 重链包括三个细胞外结构域 (α1、α2和α3)、跨膜区和胞质尾区。 FcRn在结构上与MHC I类分子类似，但由于肽结合沟阻塞使FcRn缺乏肽结合特性。 Oganesyan 等人首次报道了人FcRn的3D结构（如下图），FcRn可以分别与人IgG的Fc区域和人血清白蛋白 (HSA)结合，或同时与两种配体结合 …

We report the three-dimensional structure of human neonatal Fc receptor (FcRn) bound concurrently to its two known ligands. More particularly, we solved the crystal structure of the complex between human FcRn, wild-type human serum albumin (HSA), and a human Fc engineered for improved pharmacokinetics properties (Fc-YTE).