化学
三嗪
亲和层析
琼脂糖
共价键
连接器
配体(生物化学)
环氧氯丙烷
色谱法
三聚氯氰
芳基
生物化学
有机化学
酶
受体
操作系统
烷基
计算机科学
作者
Hamed Farzi-Khajeh,Sayna Toraby,Mostafa Akbarzadeh-Khiavi,Azam Safary,Mohammad Hossein Somi
标识
DOI:10.1016/j.chroma.2022.463559
摘要
Immunoglobulin purification from different biological fluids is considered one of the most critical steps in antibody production for diagnostic, therapeutic, and research purposes. The current study aimed to elucidate the role of the different aryl substituents in triazine-based affinity ligands on the performance of an affinity chromatography purification media to separate immunoglobulin G (IgG). The biomimetic triazine-based affinity ligand was chosen as a varied containing fix spacer and support. The sepharose beads were activated by epichlorohydrin, and five types of aryl substituents were replaced in the triazine ring and covalently immobilized to the resin surface by 1, 4-diaminobutane spacer. All affinity resins with various ligands were characterized and validated using FTIR, SEM, EDX, and microscopic images. The findings revealed that using R1=3-aminophenol and R2=3-aminophenol substituents in the triazine ring, as affinity ligands attached to the sepharose surface with a 10-atom linker CAES-6B-Cl@R1= MAF, R2= MAF (No. 4), leads to better purification of IgG from human and rabbit plasma with 22.8 mg/mL resin binding capacity in 73±5% yield and 95% of purity. All results confirmed that the designed triazine-based affinity ligands could effectively purify IgG compatible with a fast and low-cost approach.
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