Identification of the Root Cause of Visible Particle Formation in a Therapeutic Monoclonal Antibody by LC-MS-Based Approaches

IF 4.9 2区 医学 Q2 MEDICINE, RESEARCH & EXPERIMENTAL
Molecular Pharmaceutics Pub Date : 2026-10-05 Epub Date: 2026-09-23 DOI:10.1021/acs.molpharmaceut.6c00548
Amareth Lim, Andrew G. Werner, Brandon L. Doyle, William D. Holmes, Andrew W. Carr, Chi A. Nguyen, Suzanne E. Stone, Elisabeth Krug
{"title":"Identification of the Root Cause of Visible Particle Formation in a Therapeutic Monoclonal Antibody by LC-MS-Based Approaches","authors":"Amareth Lim,&nbsp;Andrew G. Werner,&nbsp;Brandon L. Doyle,&nbsp;William D. Holmes,&nbsp;Andrew W. Carr,&nbsp;Chi A. Nguyen,&nbsp;Suzanne E. Stone,&nbsp;Elisabeth Krug","doi":"10.1021/acs.molpharmaceut.6c00548","DOIUrl":null,"url":null,"abstract":"<p>Visible particles were observed for a therapeutic monoclonal antibody at pH 5.5. This pH was considered optimal for this antibody during preclinical development. To minimize the particle formation, the pH of the final drug substance was increased to 6.5. There were no visible particles at pH 6.5 initially, but visible particles started to form after 2 months. To minimize impact to the clinical program, a lyophilized formulation presentation was chosen. Subsequently, due to the desire for patient administration through subcutaneous injection for this antibody, a stable, high concentration solution formulation was needed. Thus, the pH was further increased to 7.2 to mitigate the visible particle formation. LC-MS-based approaches, including reduced LC−MS analysis and cathepsin D-targeted LC−MS Lys-C peptide map analysis, were developed to identify the root cause of the visible particle formation of this antibody at pH 5.5 to ensure the successful development of a stable solution formulation at pH 7.2. Results from studies supported by LC-MS-based analyses indicated that visible particles observed in the antibody protein A capture main pool sample at pH 5.0 were associated with cathepsin D clipping of the antibody. In contrast, visible particles observed in the purified antibody drug substance samples at pH 5.5 and pH 6.5 and in the antibody in-process samples (from the low pH viral inactivation, anion exchange chromatography, hydrophobic interaction chromatography, and tangential flow filtration unit operations) were associated with succinimide intermediate formation at an Asp residue with an Asp−Ser sequence motif in one of the complementarity-determining regions of the light chain. Understanding the root cause of the particle formation of this antibody at pH 5.5 enabled us to perform targeted experiments to rapidly develop a stable high concentration solution formulation for this antibody and meet project timelines.</p>","PeriodicalId":52,"journal":{"name":"Molecular Pharmaceutics","volume":"23 10","pages":"4960–4973"},"PeriodicalIF":4.9000,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular Pharmaceutics","FirstCategoryId":"3","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acs.molpharmaceut.6c00548","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2026/9/23 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"MEDICINE, RESEARCH & EXPERIMENTAL","Score":null,"Total":0}
引用次数: 0

Abstract

Visible particles were observed for a therapeutic monoclonal antibody at pH 5.5. This pH was considered optimal for this antibody during preclinical development. To minimize the particle formation, the pH of the final drug substance was increased to 6.5. There were no visible particles at pH 6.5 initially, but visible particles started to form after 2 months. To minimize impact to the clinical program, a lyophilized formulation presentation was chosen. Subsequently, due to the desire for patient administration through subcutaneous injection for this antibody, a stable, high concentration solution formulation was needed. Thus, the pH was further increased to 7.2 to mitigate the visible particle formation. LC-MS-based approaches, including reduced LC−MS analysis and cathepsin D-targeted LC−MS Lys-C peptide map analysis, were developed to identify the root cause of the visible particle formation of this antibody at pH 5.5 to ensure the successful development of a stable solution formulation at pH 7.2. Results from studies supported by LC-MS-based analyses indicated that visible particles observed in the antibody protein A capture main pool sample at pH 5.0 were associated with cathepsin D clipping of the antibody. In contrast, visible particles observed in the purified antibody drug substance samples at pH 5.5 and pH 6.5 and in the antibody in-process samples (from the low pH viral inactivation, anion exchange chromatography, hydrophobic interaction chromatography, and tangential flow filtration unit operations) were associated with succinimide intermediate formation at an Asp residue with an Asp−Ser sequence motif in one of the complementarity-determining regions of the light chain. Understanding the root cause of the particle formation of this antibody at pH 5.5 enabled us to perform targeted experiments to rapidly develop a stable high concentration solution formulation for this antibody and meet project timelines.

用lc - ms方法鉴定治疗性单克隆抗体中可见颗粒形成的根本原因
治疗性单克隆抗体在pH 5.5下观察到可见颗粒。在临床前开发期间,该pH值被认为是该抗体的最佳pH值。为了减少颗粒的形成,将最终原料药的pH值提高到6.5。pH 6.5时初始无可见颗粒,2个月后开始形成可见颗粒。为了尽量减少对临床项目的影响,选择了冻干制剂。随后,由于患者希望通过皮下注射该抗体,需要一种稳定、高浓度的溶液制剂。因此,pH进一步增加到7.2,以减轻可见颗粒的形成。开发了基于LC-MS的方法,包括减少LC-MS分析和组织蛋白酶d靶向LC-MS Lys-C肽图分析,以确定该抗体在pH 5.5下可见颗粒形成的根本原因,以确保在pH 7.2下成功开发稳定的溶液配方。lc - ms分析支持的研究结果表明,在pH 5.0时抗体蛋白A捕获主池样品中观察到的可见颗粒与抗体的组织蛋白酶D剪切有关。相比之下,在pH为5.5和6.5的纯化抗体原料药样品和抗体加工样品(来自低pH病毒灭活、阴离子交换色谱、疏水相互作用色谱和切向流过滤单元操作)中观察到的可见颗粒与琥珀酰亚胺中间体形成有关,这些中间体位于轻链互补决定区域之一的具有Asp - Ser序列基序的Asp残基上。了解了该抗体在pH 5.5下颗粒形成的根本原因,使我们能够进行有针对性的实验,快速开发出该抗体的稳定的高浓度溶液配方,并满足项目时间表。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Molecular Pharmaceutics
Molecular Pharmaceutics 医学-药学
CiteScore
8.00
自引率
6.10%
发文量
391
审稿时长
2 months
期刊介绍: Molecular Pharmaceutics publishes the results of original research that contributes significantly to the molecular mechanistic understanding of drug delivery and drug delivery systems. The journal encourages contributions describing research at the interface of drug discovery and drug development. Scientific areas within the scope of the journal include physical and pharmaceutical chemistry, biochemistry and biophysics, molecular and cellular biology, and polymer and materials science as they relate to drug and drug delivery system efficacy. Mechanistic Drug Delivery and Drug Targeting research on modulating activity and efficacy of a drug or drug product is within the scope of Molecular Pharmaceutics. Theoretical and experimental peer-reviewed research articles, communications, reviews, and perspectives are welcomed.
×
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:604180095
Book学术官方微信
小红书