The University of Lausanne is offering this technology for licensing or for collaboration.

The technology allows measurement of the interaction between a ligand and its receptor by atomic force microscopy. The nature of the ligand can be varied, the receptor is either a protein or nucleic acid or any compound of interest that can be bound to the support.

Development Phase :
Prototype. Reduced to practice.

Patent Status :
A provisional patent application has been filed in May 2001

Patent Attorney :
Mintz & Levin, Boston, USA

Novelty and Benefits :
The benefits of this method are manifold. Sample fixation has been simplified and is now up to 20 times faster, analysis of the AFM readings are done on-line, the cost of the material is strongly reduced and the type of protein interactions that can be analysed is greatly increased. The same set-up can be used to measure nucleic acids-proteins or nucleic acids-nucleic acids interactions. The process can easily be automated.

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

Protein affinity screening by Atomic Force Microscopy (AFM)

(Ref. Number IDF 11.01)

The Technology  :
The atomic force microscope was primarily designed to make atomic resolution images, but it recently appeared to be a very useful instrument for measuring specific interactions between bio-molecules.

The standard procedure consists in binding one molecular species onto the AFM tip (ligand) and the second (receptor) onto a flat surface such as mica or gold. The measurement of the affinity between ligand and receptor is accomplished by periodically lowering and rising the AFM tip and recording the deformations of the AFM cantilever during the process. The deflection of the cantilever at breaking point allows calculation of the binding force between the receptor and the ligand.

We propose an improved version of the technology described above. The method consists in depositing manually, by HPLC, FPLC or any other purification technique, dozens or hundreds of proteins (receptors) onto a special support. Several improvements were achieved in the deposition of the samples and the data analysis processes. These improvements allow a ten to hundred fold increase in the specimen analysis and therefore open new perspectives in protein-protein affinity screening.

Applications :
Proteomics, drug screening.