Two protein interaction peaks are observed in pharmaceutically-relevant protein (serum albumin) : disaccharide 1 : 1 and 1 : 3 (w/w) freeze-dried systems for the first time. In samples with a higher disaccharide content, the protein–protein distances are longer for both populations, while the fraction of the protein population with a shorter protein–protein distance is lower. Both factors would favor better stability against aggregation for disaccharide-rich protein formulations. This study provides direct experimental support for a “dilution” hypothesis as a potential stabilization mechanism for freeze-dried protein formulations.

中文翻译：

---

通过小角中子和 X 射线散射（SANS 和 SAXS）在冻干蛋白质：冻干保护剂（二糖）系统中检测到的两种蛋白质分子

首次在药物相关蛋白质（血清白蛋白）：二糖 1:1 和 1:3（w/w）冻干系统中观察到两个蛋白质相互作用峰。在二糖含量较高的样品中，两个群体的蛋白质-蛋白质距离都较长，而蛋白质-蛋白质距离较短的蛋白质群体的比例较低。这两个因素都有利于富含二糖的蛋白质制剂具有更好的抗聚集稳定性。这项研究为“稀释”假设作为冻干蛋白质制剂的潜在稳定机制提供了直接的实验支持。