Fusion With Post-Translational Modification Motif TRIZ Cases

Engineered platelets use antibody-guided split toxins to kill circulating tumor cells while limiting systemic side effects.

A monoclonal antibody targets free biotin over biotinylated molecules to reduce assay interference and improve analyte measurement accuracy.

Selective tail-moiety binding captures free biotin without binding biotinylated targets, improving avidin-biotin assay accuracy.

Split-intein feedback controllers use antithetic integral control to keep protein expression constant across disturbances and host conditions.

An oxygen-dependent degradation domain enables CAR units to splice in hypoxic tumors, limiting activation in normal tissues.

Engineered T cells display non-signaling anti-IL-6 binders to lower cytokine levels and reduce IL-6-linked CRS severity.

Targeting biotin’s valeric acid moiety lets the antibody capture free biotin without binding conjugated biotin, reducing assay interference.

By recognizing biotin’s valeric acid moiety, this monoclonal antibody binds free biotin without binding biotinylated molecules, reducing assay interference.

Mutations at N-intein positions 24 and/or 25 improve solubility and cleavage, enabling scalable tag-less protein recovery.

This case uses valeric-acid recognition to remove free biotin while preserving biotinylated analyte detection in assays.

A single-site glycosylated FcγRIIIa ligand separates antibody glycoforms with improved resolution and scalable chromatographic use.

Trans-splicing inteins separate affinity tags from bFGF, eliminating endotoxin contamination and reducing purification costs.

A GlycoSCORES platform uses cell-free protein synthesis and mass spectrometry to determine enzyme specificities.

Purified MAIT cells engineered with anti-CD4 receptors eliminate graft-versus-host disease risk while enhancing solid tumor infiltration.

A ribosomal platform encodes non-canonical amino acids to form stable thioether bonds for macrocyclic peptides.

Longer biotinylation domains provide structural rigidity for epitope recognition, resolving the trade-off between production efficiency and detection precision.

Segmenting fluorescent probes into small peptide tags and dye molecules resolves size constraints while enabling specific protein monitoring in living cells.

Engineered inteins resolve bacterial inclusion body formation by improving solubility and increasing yeast surface display yields.

Robust split inteins enable high-yielding protein splicing in the presence of chaotropic salts, resolving industrial scalability bottlenecks.

A chimeric endocytic receptor fuses FcγRI binding domains with signaling chains to drive antigen uptake in engineered T cells.

Segmented intein fragments accelerate splicing kinetics and improve sequence tolerance, resolving slow reaction rates in protein chemistry.

Split intein fusion proteins covalently link Mfp5 sequences into high molecular weight oligomers for enhanced underwater adhesion.