Conventional immunoassays rely on antibodies that provide high affinity, specificity, and selectivity against a target analyte.
Selection methods are used to identify Affimers that recognise α-helix mimicking
To enable multiplexed protein analysis through the use of microarrays, reliable molecules capable of specifically binding to a protein of interest with high affinity are required. Further, this specificity and affinity must be retained upon immobilization to the microarray surface.
Biosensors with high sensitivity and short time-to-result that are capable of detecting biomarkers in body fluids such as serum are an important prerequisite for early diagnostics in modern healthcare provision.
The B-cell CLL/lymphoma-2 (Bcl-2) family of proteins are important regulators of the intrinsic pathway of apoptosis, and their interactions, driven by Bcl-2 homology (BH) domains, are of great interest in cancer research.
Adhirons (commercialised as Affimer reagents) are robust, well expressing, peptide display scaffold proteins, developed as an effective alternative to traditional antibody binding proteins for highly specific molecular recognition applications. Read More
The HIF-1α/p300 protein–protein interaction plays a key role in tumor metabolism and thus represents a high value target for anticancer drug-development.
The development of novel protein-targeted MRI contrast agents crucially depends on the ability to derivatise suitable targeting moieties with a high payload of relaxation enhancer (e.g., gadolinium(III) complexes such as Gd-DOTA), without losing affinity for the target proteins.
Peptide aptamer (commercialised as Affimer) technology has the advantage over existing techniques that the reagents identified are designed for expression in eukaryotic cells.
Enhanced complement C3 incorporation into the fibrin network in diabetes is one mechanism for impaired fibrinolysis and increased thrombosis risk in this condition. Our aim was to develop new strategies to modulate fibrinolysis in diabetes by interfering with fibrin-C3 interaction.