8xj0
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8xj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xj0 OCA], [https://pdbe.org/8xj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xj0 RCSB], [https://www.ebi.ac.uk/pdbsum/8xj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xj0 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8xj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xj0 OCA], [https://pdbe.org/8xj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xj0 RCSB], [https://www.ebi.ac.uk/pdbsum/8xj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xj0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fab is a promising format for antibody drug. Therefore, efforts have been made to improve its thermal stability for therapeutic and commercial use. So far, we have attempted to introduce a disulfide bond into the Fab fragment to improve its thermal stability and demonstrated that it is possible to do this without sacrificing its biochemical function. In this study, to develop a novel stabilization strategy for Fab, we attempted to introduce a disulfide bond between the variable and constant domains and prepared three variants of Fab; H:G10C + H:P210C, L:P40C + L:E165C, and H:G10C + H:P210C + L:P40C + L:E165C. Differential scanning calorimetry measurements showed that each of these variants had improved thermal stability. In addition, the variants with two disulfide bonds demonstrated a 6.5 degrees C increase in their denaturation temperatures compared to wild-type Fab. The introduction of disulfide bonds was confirmed by X-ray crystallography, and the variants retained their antigen-binding activity. The variants were also found to be less aggregative than the wild type. Our results demonstrate that the introduction of a disulfide bond between the variable and constant domains significantly improves the thermal stability of Fab. | ||
| + | |||
| + | Stabilization of adalimumab Fab through the introduction of disulfide bonds between the variable and constant domains.,Yoshikawa M, Senda M, Nakamura H, Oda-Ueda N, Ueda T, Senda T, Ohkuri T Biochem Biophys Res Commun. 2024 Mar 12;700:149592. doi: , 10.1016/j.bbrc.2024.149592. Epub 2024 Jan 28. PMID:38295648<ref>PMID:38295648</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8xj0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of AmFab mutant - P40C/E165C (Light chain), G10C/P210C(Heavy chain)
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