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Affibody molecules are a class of engineered affinity proteins with proven potential for therapeutic, diagnostic and biotechnological applications.
In addition, we provide an overview of some of the major present and future applications for these engineered affinity proteins in biotechnology and medicine.
This review describes the integration of supramolecular interactions on the design of delivery strategies that encompass self-assembling and engineered affinity components to construct advanced biomimetic carriers for growth factor delivery.
Neutralization of leukemia-expressed GITRL by the GITR domain enhanced cytotoxicity and cytokine production of NK cells depending on activation state with NK reactivity being further largely dependent on the engineered affinity of the fusion proteins to the Fc receptor.
By using engineered affinity enhanced TCRs to these ligands, which have extended off-rates of ∼1 h compared to seconds for the wildtype TCRs, we have examined pMHCI/CD8 binding before and during TCR-engagement.
Here, we compare an antibody with the highest known engineered affinity (Kd=270 fM) to its high affinity wild-type (Kd=700 pM) through thermodynamic, kinetic, structural, and theoretical analyses.
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Engineered binding affinity, avidity and pH-sensitivity have been shown to affect binding, intracellular sorting and release, ultimately leading to increased brain uptake of the targeting vector and its associated cargo.
In the study herein, we engineered double affinity tags for facilitating purification of recombinant DGAT1 from E. coli.
We engineered high-affinity SIRPα variants with approximately 50,000-fold increased affinity for human CD47 relative to wild-type SIRPα.
In contrast, engineered higher-affinity type I IFNs did not increase antiviral potency over wild-type type I IFNs.
In contrast, engineered higher-affinity type I IFNs did not increase antiviral potency over wild-type type I IFNs.
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