CaptureSelect FcXP 亲和培养基具有很强的聚合分离能力。

IF 1.4 4区 生物学 Q4 BIOCHEMICAL RESEARCH METHODS
Wanyuan Dong, Dan Zhang, Yifeng Li
{"title":"CaptureSelect FcXP 亲和培养基具有很强的聚合分离能力。","authors":"Wanyuan Dong,&nbsp;Dan Zhang,&nbsp;Yifeng Li","doi":"10.1016/j.pep.2024.106503","DOIUrl":null,"url":null,"abstract":"<div><p>Protein A affinity chromatography has been widely used for initial product capture in recombinant antibody/Fc-fusion purification. However, in general Protein A lacks the capability of separating aggregates (unless the aggregates are too large to enter the pores of resin beads or have their Protein A binding sites buried, in which case the aggregates do not bind). In the current work, we demonstrated that CaptureSelect FcXP affinity medium exhibited strong aggregate separation capability and effectively removed aggregates under pH or conductivity gradient elution in two bispecific antibody (bsAb) cases. For these two cases, aggregate contents were reduced from &gt;16% and &gt;22% (in the feed) to &lt;1% and &lt;5% (in the eluate) for the first and second bsAbs, respectively. While more case studies are required to further demonstrate FcXP's superiority in aggregate removal, findings from the current study suggest that FcXP can potentially be a better alternative than Protein A for product capture in cases where aggregate content is high.</p></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"220 ","pages":"Article 106503"},"PeriodicalIF":1.4000,"publicationDate":"2024-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"CaptureSelect FcXP affinity medium exhibits strong aggregate separation capability\",\"authors\":\"Wanyuan Dong,&nbsp;Dan Zhang,&nbsp;Yifeng Li\",\"doi\":\"10.1016/j.pep.2024.106503\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Protein A affinity chromatography has been widely used for initial product capture in recombinant antibody/Fc-fusion purification. However, in general Protein A lacks the capability of separating aggregates (unless the aggregates are too large to enter the pores of resin beads or have their Protein A binding sites buried, in which case the aggregates do not bind). In the current work, we demonstrated that CaptureSelect FcXP affinity medium exhibited strong aggregate separation capability and effectively removed aggregates under pH or conductivity gradient elution in two bispecific antibody (bsAb) cases. For these two cases, aggregate contents were reduced from &gt;16% and &gt;22% (in the feed) to &lt;1% and &lt;5% (in the eluate) for the first and second bsAbs, respectively. While more case studies are required to further demonstrate FcXP's superiority in aggregate removal, findings from the current study suggest that FcXP can potentially be a better alternative than Protein A for product capture in cases where aggregate content is high.</p></div>\",\"PeriodicalId\":20757,\"journal\":{\"name\":\"Protein expression and purification\",\"volume\":\"220 \",\"pages\":\"Article 106503\"},\"PeriodicalIF\":1.4000,\"publicationDate\":\"2024-05-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Protein expression and purification\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1046592824000755\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein expression and purification","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1046592824000755","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
引用次数: 0

摘要

蛋白 A 亲和层析已被广泛用于重组抗体/Fc 融合纯化的初始产物捕获。然而,一般来说,蛋白 A 缺乏分离聚集体的能力(除非聚集体太大,无法进入树脂珠的孔中,或者其蛋白 A 结合位点被埋没,在这种情况下,聚集体不会结合)。在目前的工作中,我们证明了 CaptureSelect FcXP 亲和培养基具有很强的聚集体分离能力,并在两种双特异性抗体(bsAb)情况下,在 pH 或电导梯度洗脱条件下有效去除聚集体。在这两种情况下,第一种和第二种双特异性抗体的聚集体含量分别从进样中的 16% 和 22% 降至洗脱液中的 1% 和 5% 。虽然还需要更多的案例研究来进一步证明 FcXP 在去除骨料方面的优越性,但目前的研究结果表明,在骨料含量较高的情况下,FcXP 有可能成为比蛋白质 A 更好的产品捕获替代品。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
CaptureSelect FcXP affinity medium exhibits strong aggregate separation capability

Protein A affinity chromatography has been widely used for initial product capture in recombinant antibody/Fc-fusion purification. However, in general Protein A lacks the capability of separating aggregates (unless the aggregates are too large to enter the pores of resin beads or have their Protein A binding sites buried, in which case the aggregates do not bind). In the current work, we demonstrated that CaptureSelect FcXP affinity medium exhibited strong aggregate separation capability and effectively removed aggregates under pH or conductivity gradient elution in two bispecific antibody (bsAb) cases. For these two cases, aggregate contents were reduced from >16% and >22% (in the feed) to <1% and <5% (in the eluate) for the first and second bsAbs, respectively. While more case studies are required to further demonstrate FcXP's superiority in aggregate removal, findings from the current study suggest that FcXP can potentially be a better alternative than Protein A for product capture in cases where aggregate content is high.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Protein expression and purification
Protein expression and purification 生物-生化研究方法
CiteScore
3.70
自引率
6.20%
发文量
120
审稿时长
32 days
期刊介绍: Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信