Binding epitope for recognition of human TRPM4 channel by monoclonal antibody M4M. Wei, S., Behn, J., Poore, C. P., Low, S. W., Nilius, B., Fan, H., & Liao, P. Scientific Reports, 12(1):19562, November, 2022. ![Binding epitope for recognition of human TRPM4 channel by monoclonal antibody M4M [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Abstract Mouse monoclonal antibody M4M was recently designed to block human TRPM4 channel. The polypeptide for generating M4M is composed of peptide A1 between the transmembrane segment 5 (S5) and the pore, and a second peptide A2 between the pore and the transmembrane segment 6 (S6). Using peptide microarray, a 4-amino acid sequence EPGF within the A2 was identified to be the binding epitope for M4M. Substitution of EPGF with other amino acids greatly reduced binding affinity. Structural analysis of human TRPM4 structure indicates that EPGF is located externally to the channel pore. A1 is close to the EPGF binding epitope in space, albeit separated by a 37-amino acid peptide. Electrophysiological study reveals that M4M could block human TRPM4, but with no effect on rodent TRPM4 which shares a different amino acid sequence ERGS for the binding motif. Our results demonstrate that M4M is a specific inhibitor for human TRPM4.
@article{wei_binding_2022,
title = {Binding epitope for recognition of human {TRPM4} channel by monoclonal antibody {M4M}},
volume = {12},
issn = {2045-2322},
url = {https://www.nature.com/articles/s41598-022-22077-4},
doi = {10.1038/s41598-022-22077-4},
abstract = {Abstract
Mouse monoclonal antibody M4M was recently designed to block human TRPM4 channel. The polypeptide for generating M4M is composed of peptide A1 between the transmembrane segment 5 (S5) and the pore, and a second peptide A2 between the pore and the transmembrane segment 6 (S6). Using peptide microarray, a 4-amino acid sequence EPGF within the A2 was identified to be the binding epitope for M4M. Substitution of EPGF with other amino acids greatly reduced binding affinity. Structural analysis of human TRPM4 structure indicates that EPGF is located externally to the channel pore. A1 is close to the EPGF binding epitope in space, albeit separated by a 37-amino acid peptide. Electrophysiological study reveals that M4M could block human TRPM4, but with no effect on rodent TRPM4 which shares a different amino acid sequence ERGS for the binding motif. Our results demonstrate that M4M is a specific inhibitor for human TRPM4.},
language = {en},
number = {1},
urldate = {2022-11-21},
journal = {Scientific Reports},
author = {Wei, Shunhui and Behn, Julian and Poore, Charlene Priscilla and Low, See Wee and Nilius, Bernd and Fan, Hao and Liao, Ping},
month = nov,
year = {2022},
keywords = {Application - Antibody Validation / Epitope Mapping, Application - Protein Target Binder Studies, PEPperCHIP - Customized - Cyclic constrained, PEPperMAP - Substitution Scan},
pages = {19562},
}
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Substitution of EPGF with other amino acids greatly reduced binding affinity. Structural analysis of human TRPM4 structure indicates that EPGF is located externally to the channel pore. A1 is close to the EPGF binding epitope in space, albeit separated by a 37-amino acid peptide. Electrophysiological study reveals that M4M could block human TRPM4, but with no effect on rodent TRPM4 which shares a different amino acid sequence ERGS for the binding motif. 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The polypeptide for generating M4M is composed of peptide A1 between the transmembrane segment 5 (S5) and the pore, and a second peptide A2 between the pore and the transmembrane segment 6 (S6). Using peptide microarray, a 4-amino acid sequence EPGF within the A2 was identified to be the binding epitope for M4M. Substitution of EPGF with other amino acids greatly reduced binding affinity. Structural analysis of human TRPM4 structure indicates that EPGF is located externally to the channel pore. A1 is close to the EPGF binding epitope in space, albeit separated by a 37-amino acid peptide. Electrophysiological study reveals that M4M could block human TRPM4, but with no effect on rodent TRPM4 which shares a different amino acid sequence ERGS for the binding motif. 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