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Updated: Jul 2, 2025

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氨酸和普鲁兰的组合揭示了稳定机制对不同冷解蛋白的选择性作用

Khanh T T Nguyen¹, Daan Zillen¹, Alessia Lasorsa²

¹Department of Pharmaceutical Technology and Biopharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, the Netherlands.

International journal of pharmaceutics

|February 26, 2024

概括

氨酸和氨酸混合物通过冷化稳定乳酸脱酶 (LDH) 和β-galactosidase (β-gal) 等酶. 最佳稳定性取决于氨酸/普卢兰比率和储存条件,影响酶活性.

科学领域:

生物化学生化学
材料科学材料科学材料科学
制药科学制药科学

背景情况:

酶稳定性对于生物制药配方至关重要.
解热化是一种稳定蛋白质的常见技术.
氨酸和普鲁兰是酶稳定的潜在辅助剂.

研究的目的:

为了评估乳酸脱酶 (LDH) 和β-galactosidase (β-gal) 的稳定,使用阿尔金因/普卢兰 (A/P) 混合物.
评估A/P重量比对酶稳定性和配方特性的影响.
为了研究玻璃状和状状态在酶降解中的作用.

主要方法:

在各种A/P重量比下,LDH和β-gal的冷化.
评估物理化学特性,包括玻璃过渡温度.
在不同相对湿度和温度条件下储存后,酶活性测定.
固态核磁共振 (ssNMR) 光谱检测分子相互作用.

主要成果:

降低A/P比率增加了配方的玻璃过渡温度.
在A/P比为4/6或更低时,氨酸结晶被阻止.
在特定的储存条件下,在2/8的A/P比率下,LDH活性最好保持.
在A/P比为8/2和2/8.8时,β-gal活性保持良好.
在玻璃状和状状态之间,酶降解率有所不同,LDH在状状态下更容易降解.

结论:

在A/P矩阵中稳定LDH需要达到玻璃状状态.
LDH和β-gal的差异稳定可能归因于它们与氨酸的特定相互作用.
在某些条件下,与Pullulan相比,阿基尼在某些条件下表现出更好的稳定作用.

关键词:

生物制药产品生物制药辅助物质辅助物质辅助物质互动互动互动互动稳定的稳定性稳定的稳定性玻璃化是一种玻璃化过程.取代水的替代方法固态NMR是一种固态NMR.

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