ArticleJournal of medicinal chemistry2024
Experimental and Computational Studies on Domain-Swapped Structure Stabilization of an Antibody Light Chain by Disulfide Bond Introduction.
Article in Journal of medicinal chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Development of different platforms would be useful for designing functional antibodies to improve the efficiency of antibody-based drugs. Three-dimensional domain swapping (3D-DS) may occur in the variable region of antibody light chain #4C214A, and a pair of domain-swapped dimers may interact with each other to form a tetramer. In this study, to stabilize the 3D-DS dimer structure in #4C214A, Val2 in strand A (swapping region) and Thr97 in strand G were replaced with Cys residues, generating #4 V2C/T97C/C214A with a Cys2-Cys97 disulfide bond that cross-links strands A and G of different protomers. The #4 V2C/T97C/C214A tetramer did not dissociate into monomers at low protein concentration (6 μM); however, some of the tetramers were converted to monomers by disulfide bond reduction. Two-dimensional free energy profile analysis for the tetramerization of two 3D-DS dimers was performed by molecular dynamics simulation. These results show that disulfide bond introduction is useful for controlling the dimerization/dissociation of the variable region through 3D-DS.
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