A Fast, Reliable Method for Predicting Allosteric Coupling for Targeted Drug Design and Analysis of Protein Stability

Web Published:
11/30/2011
Description:

 

Princeton Docket # 10-2609

 

Researchers at the Lewis-Sigler Institute for Integrative Genomics, Princeton University have developed a novel method for computing information about a protein¿s preferred three-dimensional structure from its amino acid sequence.  Using a simple set of assumptions, the method utilizes the pattern of hydrophobicity in the protein¿s sequence to calculate the optimal and nearly optimal structures for that sequence in seconds.  This information may be utilized as a guidance system for many applications, including targeted drug design. The method may also be used in the detection of allosteric coupling and the detection of structural instability. In the case of targeted drug design, the method will allow for the identification of regions on a protein that are strongly coupled conformationally to another region of interest. Drugs may be designed based on results to target one part of the protein with the aim of allosterically disrupting the other part. It is also possible that this method may allow one to predict the effects of phosphorylation or other covalent modifications of proteins or to design new proteins of novel structure for industrial or medical purposes.

 

Applications       

·         Allosteric coupling prediction for targeted drug design

·         Structural instability prediction

·         Effect prediction of phosphorylation or other covalent modifications of proteins

·         Novel protein structure design

 

Advantages         

·         Fast computation

·         Allosteric coupling prediction as transformative new capability

 

 

Publication
England JL. Allostery in protein domains reflects a balance of steric and hydrophobic effects. Structure. 2011 Jul 13;19(7):967-75.

 

Inventor
Jeremy England is Assistant Professor of Physics at Massachusetts Institute of Technology (MIT). Before his appointment in MIT, he was a lecturer and research fellow at Princeton University.  Dr. England's research is directed towards understanding the patterns of organization in space and time that form the basis of life at the molecular level.

 

Intellectual Property status

Patent protection is pending.

Patent Information:
For Information, Contact:
Laurie Tzodikov
Licensing Associates
Princeton University
tzodikov@Princeton.EDU
Inventors:
Jeremy England
Keywords:
computers/software
drug discovery
life science research tools