Prof. Kini's Laboratory








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Protein-Protein Interaction Sites

Protein-protein interactions are crucial to almost every physiological and pharmacological process. Identification of a protein-protein interaction site is an important step that has significant potential to clarify structure-function relationships of proteins and drug design.  We have obtained 9 US patents on this technology and another 6 applications are pending. Some of these patents are licensed to a Singapore company. Our significant contributions are given below.

  • We identified the presence of proline residues as common structural elements in the flanking segments of  protein - protein  interaction sites and defined a hypothetical structural role for these prolines based on their physicochemical properties. This is the first time any such common structural features have been identified in the flanking segments of interaction sites. I believe this basic finding will reach the textbooks. We have provided experimental evidence for this finding in two orthogonal directions.


  • We exploited the above finding, to develop a novel method to design and develop short synthetic peptides with high potency of biological activities. Based on this universal design, the potency of peptides can be enhanced by 10-20 folds.





  • We also developed a novel method to identify protein-protein interaction sites as a corollary to the presence of prolines in the flanking segments. Accordingly, potential protein-protein interaction sites can be identified directly from the amino acid sequence of a protein without any input from secondary or tertiary structure of the protein. Using this method, we have identified the functional sites of more than 15 structurally and functionally unrelated proteins. This indicates the robustness of our simple and straightforward method.



Key Publications

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