ULTRA-STABLE STREPTAVIDIN - Isis Project No 4258
The University of Oxford has engineered a streptavidin mutant that binds biotin-conjugates more stably than wild-type streptavidin.
The Oxford Invention
The new “Traptavidin” mutant has the potential to replace streptavidin in many applications, including arrays, surface-plasmon-resonance, point-of-care diagnostics, immunoassays, purification and imaging.
The streptavidin-biotin system is already widely used in many fields and Traptavidin increases the effectiveness of streptavidin by making the interaction more stable, and effective in a wider variety of conditions.
Traptavidin has the potential to replace streptavidin in many of its applications due to its;
- 10-fold decreased off-rate;
- Increased thermostability;
- Increased mechanical stability;
- Similar ease of expression.
Streptavidin is one of the most widely used tools in molecular biological research, due to its extraordinarily strong affinity for biotin. The dissociation constant (KD) of the biotin-streptavidin complex is on the order of 10-14 M, which is one of the highest affinity interactions known in nature.
This affinity can be used to attach various biomolecules to one another or onto a solid support, for many uses including nano-assembly, immunoassays, purification and imaging.
Despite the strength of the streptavidin-biotin interaction, the stability of this interaction is limiting for many applications because it has been shown to fail in certain conditions including low pH, when attaching to nanoparticles and in the presence of mild shear force, as well as in the path of molecular motors and at high temperatures. Therefore, the availability of the first mutant produced with stronger binding than wild-type streptavidin is highly attractive.
The Oxford invention is the subject of an international patent application. Isis would like to talk to companies interested in developing the commercial opportunity. Please contact the Isis Project Manager.