A comprehensive evaluation of arginine and its derivatives as protein formulation stabilizers

精氨酸 化学 盐酸盐 单体 胶体 蛋白质聚集 色谱法 生物物理学 生物化学 有机化学 氨基酸 聚合物 生物
作者
Shavron Hada,Urmila Burlakoti,Ki Hyun Kim,Ji Soo Han,Min Ji Kim,Nam Ah Kim,Seong Hoon Jeong
出处
期刊:International Journal of Pharmaceutics [Elsevier BV]
卷期号:647: 123545-123545 被引量:2
标识
DOI:10.1016/j.ijpharm.2023.123545
摘要

Arginine and its derivatives (such as arginine ethyl ester and acetyl arginine) have varying degrees of protein aggregation suppressor effect across different protein solutions. To understand this performance ambiguity, we evaluated the activity of arginine, acetyl arginine, and arginine ethyl ester for aggregation suppressor effect against human intravenous immunoglobulin G (IgG) solution at pH 4.8. Both arginine and its cationic derivative arginine ethyl ester in their hydrochloride salt forms significantly reduced the colloidal and conformational stability (reduced kd and Tm) of IgG. Consequently, the monomer content was decreased with an increase in subvisible particulates after agitation or thermal stress. Furthermore, compared to arginine, arginine ethyl ester with one more cationic charge and hydrochloride salt form readily precipitated IgG at temperatures higher than 25 °C. On the contrary, acetyl arginine, which mostly exists in a neutral state at pH 4.8, efficiently suppressed the formation of subvisible particles retaining a high amount of monomer owing to its higher colloidal and conformational stability. Concisely, the charged state of additives significantly impacts protein stability. This study demonstrated that contrary to popular belief, arginine and its derivatives may either enhance or suppress protein aggregation depending on their net charge and concentration.
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