Polymorphic distribution of proteins in solution by mass spectrometry: The analysis of insulin analogues

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• 作者：Maely P. Fá ; vero-Retto^a ; ^d ; ¹ ; Luiz Henrique Guerreiro^a ; ^e ; ¹ ; Cá ; ssio M. Pessanha^a ; ¹ ; Leonardo C. Palmieri^a ; ¹ ; Luí ; s Maurí ; cio T.R. Lima^a ; ^b ; ^c ; ^{Mauricio@pharma.ufrj.br}
• 关键词：Human insulin ; Oligomer ; Ion mobility spectrometry ; Mass spectrometry ; Biosimilar ; Biopharmaceuticals
• 刊名：Biologicals
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：45
• 期：Complete
• 页码：69-77
• 全文大小：3119 K
• 卷排序：45

文摘

Proteins can populate a variety of conformational and oligomeric states. CD, SEC, MALDI-ToF and crystallography display limited access to equilibrium conformational diversity. Ion mobility spectrometry (IMS) evidenced dissimilar conformational and oligomeric distribution of insulin. IMS showed sensitive to variables such as solution composition and sequence variants. IMS-MS may be considered a tool in profiling the oligomeric and conformational plasticity of biopharmaceuticals.