CAS OpenIR
A minimalist peptide ligand for IgG by minimizing the binding domain of protein A
Wang, Weiying1,2; Hao, Dongxia2; Ge, Jia2; Zhao, Lan2; Huang, Yongdong2; Zhu, Kai2; Wu, Xvexing2; Su, Zhiguo2; Yu, Rong1; Ma, Guanghui2
2019-11-15
Source PublicationBIOCHEMICAL ENGINEERING JOURNAL
ISSN1369-703X
Volume151Pages:8
Abstract

Large scale application of antibody related drug has been promoting the development of short ligand with low cost and high stability for affinity chromatographic purification of immunoglobulin G (IgG). This study presents a strategy to design a short peptide ligand by minimizing the IgG binding portion from a commercial ligand of Protein A. A short hexapeptide (FYEILH) was thus screened out by the real screening technique of STD-NMR. It presented a comparable binding activity to Protein A, with the dissociation constant (K-d) of 1.8 x 10(-6) mol/L, the static binding capacity of 49.7 mg/mL, and the purity of 94% for hIgG from chromatographic purification of serum feedstock in a single step. Epitope mapping analysis by STD-NMR indicated that the carboxy groups of the charged residue E (glutamic acid) in FYEILH was the most adjacent part in binding with hIgG molecule and thus the electronic interactions among them was the dominating binding mechanism. Such mechanism was a little different from Protein A and consequently leaded to its much milder chromatographic conditions of loading at pH 6.0 and eluting at 0.5 mol/L NaCl. The study provided a strategy of reducing larger binding domains of huge Protein A molecule to smaller functional peptide ligand, and offered a potential alternative ligand with low synthesis cost for IgG purification.

KeywordAffinity Purification Chromatography Minimalist Peptide Protein a Igg Rational Design
DOI10.1016/j.bej.2019.107327
Language英语
WOS KeywordCarbohydrate-mimetic Peptide ; Affinity-chromatography ; Fc-binding ; Monoclonal-antibodies ; Immunoglobulin-g ; Std-nmr ; Purification ; Design ; Capacity ; Epitope
Funding ProjectBeijing Municipal Natural Science Foundation[L160012] ; National Natural Science Foundation of China[21676275] ; National Natural Science Foundation of China[21336010]
WOS Research AreaBiotechnology & Applied Microbiology ; Engineering
WOS SubjectBiotechnology & Applied Microbiology ; Engineering, Chemical
Funding OrganizationBeijing Municipal Natural Science Foundation ; National Natural Science Foundation of China
WOS IDWOS:000518140400033
PublisherELSEVIER
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/39495
Collection中国科学院过程工程研究所
Corresponding AuthorHao, Dongxia; Yu, Rong; Ma, Guanghui
Affiliation1.Sichuan Univ, West China Sch Pharm, Key Lab Drug Targeting & Drug Delivery Syst, Minist Educ, Chengdu 610041, Sichuan, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China
Recommended Citation
GB/T 7714
Wang, Weiying,Hao, Dongxia,Ge, Jia,et al. A minimalist peptide ligand for IgG by minimizing the binding domain of protein A[J]. BIOCHEMICAL ENGINEERING JOURNAL,2019,151:8.
APA Wang, Weiying.,Hao, Dongxia.,Ge, Jia.,Zhao, Lan.,Huang, Yongdong.,...&Ma, Guanghui.(2019).A minimalist peptide ligand for IgG by minimizing the binding domain of protein A.BIOCHEMICAL ENGINEERING JOURNAL,151,8.
MLA Wang, Weiying,et al."A minimalist peptide ligand for IgG by minimizing the binding domain of protein A".BIOCHEMICAL ENGINEERING JOURNAL 151(2019):8.
Files in This Item:
File Name/Size DocType Version Access License
A minimalist peptide(1375KB)期刊论文出版稿限制开放CC BY-NC-SAApplication Full Text
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Wang, Weiying]'s Articles
[Hao, Dongxia]'s Articles
[Ge, Jia]'s Articles
Baidu academic
Similar articles in Baidu academic
[Wang, Weiying]'s Articles
[Hao, Dongxia]'s Articles
[Ge, Jia]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Wang, Weiying]'s Articles
[Hao, Dongxia]'s Articles
[Ge, Jia]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.