Compatibility between Proteins and Polysaccharide Excipients in Oral Delivery Tablets

多糖 相容性(地球化学) 化学 药理学 色谱法 医学 生物化学 材料科学 复合材料
作者
Meng-Jia Jin,Zhen-Yi Jing,Lei Liu,Zheng AiPing,Haibin Wang,Wei‐Jie Fang
出处
期刊:Molecular Pharmaceutics [American Chemical Society]
标识
DOI:10.1021/acs.molpharmaceut.4c01413
摘要

The development of oral protein biopharmaceuticals has gradually become a hot area of research. Currently, most of the added excipients are oral excipients used in traditional small molecule drugs, such as starch and lactose. However, the interaction between proteins and oral excipients has not received much attention. For example, the interaction may have an effect on protein stability, efficacy, etc. Herein, we observed a strong interaction between protein and sodium carboxymethyl starch (CMS), a common disintegrator in oral formulations of small molecule drugs. CMS can cause the complete disappearance of a free soluble protein in trastuzumab (TRA) tablets after reconstituted, as detected by size-exclusion high-performance liquid chromatography. While the other two polysaccharides with similar structures, hydroxyethyl starch and methylcellulose, exhibited no effect on the soluble TRA concentration. CMS produces an electrostatic interaction with TRA in a certain pH range, which affects the soluble protein monomer concentration and solution turbidity, increases the hydrophobicity of the TRA-CMS complex, and reduces the thermal stability of TRA, without changing its biological activity detected by an enzyme-linked immunosorbent assay. Thus, the CMS and TRA electrostatic binding is reversible, and CMS has a potential application in sustained release in oral monoclonal antibody (mAb) and protein delivery tablets. Mixed solutions of infliximab and etanercept (a fusion protein) with CMS at different pH were also studied by SE-HPLC. The results showed that the concentration of the free soluble protein detected by SE-HPLC was significantly and universally reduced when pH was below the isoelectric point, where the positively charged protein forms a strong electrostatic interaction with the negatively charged CMS. The structural characteristics of the protein (such as surface charge, surface hydrophobicity, etc.) should be fully considered in selecting the appropriate excipients for protein biopharmaceutical tablets.
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
PDF的下载单位、IP信息已删除 (2025-6-4)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
刚刚
orixero应助111采纳,获得10
1秒前
2秒前
柚子哟哟完成签到,获得积分10
3秒前
CipherSage应助清爽雪枫采纳,获得10
3秒前
SMILE121235完成签到,获得积分10
3秒前
温婉的凝丹完成签到 ,获得积分10
3秒前
Jasper应助布曲采纳,获得10
4秒前
搜集达人应助科研工作者采纳,获得10
4秒前
6秒前
Alexander发布了新的文献求助10
6秒前
量子星尘发布了新的文献求助10
7秒前
Y垚完成签到,获得积分10
8秒前
友好小土豆完成签到,获得积分10
9秒前
第七封信发布了新的文献求助10
9秒前
huhuhu发布了新的文献求助10
11秒前
TIWOSS发布了新的文献求助10
11秒前
14秒前
14秒前
美满的芝麻完成签到,获得积分10
15秒前
15秒前
Owen应助transhuman采纳,获得10
16秒前
18秒前
Roy完成签到,获得积分10
19秒前
111发布了新的文献求助10
19秒前
待定发布了新的文献求助10
19秒前
Qyyy完成签到,获得积分10
20秒前
20秒前
HX11发布了新的文献求助10
22秒前
酷波er应助负责的孤菱采纳,获得10
23秒前
shinn发布了新的文献求助10
24秒前
搞怪唯雪完成签到,获得积分10
24秒前
Docsiwen完成签到 ,获得积分10
24秒前
NexusExplorer应助科研工作者采纳,获得10
25秒前
蒸馏水完成签到,获得积分10
25秒前
wjx发布了新的文献求助30
26秒前
Alexander完成签到,获得积分20
26秒前
26秒前
28秒前
量子星尘发布了新的文献求助10
29秒前
高分求助中
The Oxford Encyclopedia of the History of Modern Psychology 2000
Chinesen in Europa – Europäer in China: Journalisten, Spione, Studenten 1200
Deutsche in China 1920-1950 1200
Astrochemistry 1000
Mineral Deposits of Africa (1907-2023): Foundation for Future Exploration 800
Electron microscopy study of magnesium hydride (MgH2) for Hydrogen Storage 800
Learning to Listen, Listening to Learn 570
热门求助领域 (近24小时)
化学 材料科学 医学 生物 工程类 有机化学 物理 生物化学 纳米技术 计算机科学 化学工程 内科学 复合材料 物理化学 电极 遗传学 量子力学 基因 冶金 催化作用
热门帖子
关注 科研通微信公众号,转发送积分 3874284
求助须知:如何正确求助?哪些是违规求助? 3416551
关于积分的说明 10699691
捐赠科研通 3140750
什么是DOI,文献DOI怎么找? 1733005
邀请新用户注册赠送积分活动 835620
科研通“疑难数据库(出版商)”最低求助积分说明 782131