The University of Lausanne is offering this technology for licensing or for collaboration.
The technology allows to covalently label proteins in living cells, by fusion proteins and addition of the label to the culture medium
Development Phase :
Proof of principle
Patent Status :
A provisional patent application has been filed on April 10, 2001
Patent Attorney : Mintz & Levin, Boston, USA
Novelty and Benefits :
- The label is covalently linked to the fusion protein of interest
- There are no limitations regarding the labels that can be employed, although they have to be cell permeable.
- The organism of interest can be labelled in vitro and grown for later studies, by controlled addition of the label
Additional information is available upon request.
Contact :
Marjory Hunt, PhD
Tel: +41-21-314-4958
fax: +41-21-314-4957
Pactt
Office of Technology Transfer
University of Lausanne and University Hospitals
21, Rue du Bugnon
Ch-1005 Lausanne
e-mail: marjory.hunt@hospvd.ch
Intracellular Protein Labelling
(Ref. Number IDF 7.01)
The Technology :
The free access to the open reading frames of an increasing number of organisms creates the opportunity to characterise the movement, interactions and chemical microenvironment of every protein inside the cell. Most strategies that aim at realising this objective are based on the construction of a fusion protein that, upon changes in the environment of the coupled protein, elicits a physical, physiological or chemical response. Examples include the yeast-two hybrid system, Split-Ubiquitin and GFP fusion proteins. However, all these techniques have various limitations and we therefore propose a general method to specifically and covalently label fusion proteins in living cells, with small synthetic molecules capable of sensing and inducing changes in the environment of the labelled fusion protein. The specific attachment of the synthetic probe to the fusion protein is based on the unusual mechanism of the human DNA repair enzyme O6-alkylguanine DNA alkyltransferase (hAGT), which irreversibly transfers the alkyl group from its substrate, O6-alkylguananine, to one of its cysteine residues. This method should open up completely new ways of studying and manipulating proteins in living cells.
Applications :
This technology will allow scientists to study protein synthesis, intracellular migration and protein interactions. It will also allow the study of metabolic pathways and the chemical microenvironment of proteins, for example the fusion protein can be used as an intracellular ion or pH meter. This technology should be useful in the areas of proteomics and drug development.
This technology should be of interest to companies developing research tools for fundamental and applied research.