Artificial leucine rich repeats as new scaffolds for protein design

Hemda Baabur-Cohen, Subashini Dayalan, Inbal Shumacher, Rivka Cohen-Luria, Gonen Ashkenasy

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


The leucine rich repeat (LRR) motif that participates in many biomolecular recognition events in cells was suggested as a general scaffold for producing artificial receptors. We describe here the design and first total chemical synthesis of small LRR proteins, and their structural analysis. When evaluating the tertiary structure as a function of different number of repeating units (1-3), we were able to find that the 3-repeats sequence, containing 90 amino acids, folds into the expected structure.

Original languageEnglish
Pages (from-to)2372-2375
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Issue number8
StatePublished - 15 Apr 2011


  • Leucine rich repeat proteins
  • Native chemical ligation
  • Peptides
  • Protein design


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