Effects of Salts from the Hofmeister Series on the Conformational Stability, Aggregation Propensity, and Local Flexibility of an IgG1 Monoclonal Antibody

Biochemistry ◽  
2013 ◽  
Vol 52 (19) ◽  
pp. 3376-3389 ◽  
Author(s):  
Ranajoy Majumdar ◽  
Prakash Manikwar ◽  
John M. Hickey ◽  
Hardeep S. Samra ◽  
Hasige A. Sathish ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Conformational Stability ◽  
Hofmeister Series ◽  
Aggregation Propensity ◽  
Igg1 Monoclonal Antibody ◽  
Local Flexibility

scholarly journals High-Throughput Biophysical Analysis and Data Visualization of Conformational Stability of an IgG1 Monoclonal Antibody After Deglycosylation

2013 ◽  
Vol 102 (11) ◽  
pp. 3942-3956 ◽  
Author(s):  
Mohammad A. Alsenaidy ◽  
Jae Hyun Kim ◽  
Ranajoy Majumdar ◽  
David D. Weis ◽  
Sangeeta B. Joshi ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Data Visualization ◽  
High Throughput ◽  
Conformational Stability ◽  
Igg1 Monoclonal Antibody ◽  
Biophysical Analysis

scholarly journals Development of Human Monoclonal Antibody for Claudin-3 Overexpressing Carcinoma Targeting

Biomolecules ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 51 ◽  
Author(s):  
Hobin Yang ◽  
Hayeon Park ◽  
Yong Jin Lee ◽  
Jun Young Choi ◽  
TaeEun Kim ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Transmembrane Domain ◽  
Malignant Tumors ◽  
Human Monoclonal Antibody ◽  
Cross Reactivity ◽  
Drug Conjugates ◽  
Igg1 Monoclonal Antibody ◽  
Potential Biomarker ◽  
Human Igg1 ◽  
Mediate Cell

Most malignant tumors originate from epithelial tissues in which tight junctions mediate cell–cell interactions. Tight junction proteins, especially claudin-3 (CLDN3), are overexpressed in various cancers. Claudin-3 is exposed externally during tumorigenesis making it a potential biomarker and therapeutic target. However, the development of antibodies against specific CLDN proteins is difficult, because CLDNs are four-transmembrane domain proteins with high homology among CLDN family members and species. Here, we developed a human IgG1 monoclonal antibody (h4G3) against CLDN3 through scFv phage display using CLDN3-overexpressing stable cells and CLDN3-embedded lipoparticles as antigens. The h4G3 recognized the native conformation of human and mouse CLDN3 without cross-reactivity to other CLDNs. The binding kinetics of h4G3 demonstrated a sub-nanomolar affinity for CLDN3 expressed on the cell surface. The h4G3 showed antibody-dependent cellular cytotoxicity (ADCC) according to CLDN3 expression levels in various cancer cells by the activation of FcγRIIIa (CD16a). The biodistribution of h4G3 was analyzed by intravenous injection of fluorescence-conjugated h4G3 which showed that it localized to the tumor site in xenograft mice bearing CLDN3-expressing tumors. These results indicate that h4G3 recognizes CLDN3 specifically, suggesting its value for cancer diagnosis, antibody-drug conjugates, and potentially as a chimeric antigen receptor (CAR) for CLDN3-expressing pan-carcinoma.

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