Artificial Receptors

​

Design and synthesis of artificial protein receptors. The de-novo design of new protein structures may shine light on the basic principles that govern protein folding, protein-protein interactions, and interactions with other biomolecules. It may thus facilitate the development of devices for biotechnology applications, such as sensors and catalysts. Of special interest is the design of proteins that contain large and shallow solvent exposed surfaces readily available for multiple intermol​ecular interactions. We set the goal to discover such protein scaffolds using dynamic combinatorial libraries (DCLs). As a first step towards this aim, we have studied recently the design of consensus sequence Leucine Rich Repeat (LRR) proteins, and their total chemical synthesis. By evaluating their tertiary structure as a function of different number of repeating units, we were able to find several short sequences, containing up to 90 amino acids, that fold into the correct structure.

​ 

1. M. Eisenberg, I. Shumacher, R. Cohen-Luria, G. Ashkenasy “ Dynamic Combinatorial Libraries of Artificial Repeat Proteins" Bioorgan. Med. Chem. 2013, 21, 3450-3457.

2. H. Baabur, S. Dayalan, I. Shumacher, R. Cohen-Luria, G. Ashkenasy “Artificial Leucine Rich Repeats as New Scaffold for Protein Design" Bioorg. Med. Chem. Lett. 2011, 21, 2372-2375.