Allosteric modulation of protein oligomerization: An emerging approach to drug design

Ronen Gabizon, Assaf Friedler*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

44 Scopus citations


Many disease-related proteins are in equilibrium between different oligomeric forms. The regulation of this equilibrium plays a central role in maintaining the activity of these proteins in vitro and in vivo. Modulation of the oligomerization equilibrium of proteins by molecules that bind preferentially to a specific oligomeric state is emerging as a potential therapeutic strategy that can be applied to many biological systems such as cancer and viral infections. The target proteins for such compounds are diverse in structure and sequence, and may require different approaches for shifting their oligomerization equilibrium. The discovery of such oligomerization-modulating compounds is thus achieved based on existing structural knowledge about the specific target proteins, as well as on their interactions with partner proteins or with ligands. In silico design and combinatorial tools such as peptide arrays and phage display are also used for discovering compounds that modulate protein oligomerization. The current review highlights some of the recent developments in the design of compounds aimed at modulating the oligomerization equilibrium of proteins, including the "shiftides" approach developed in our lab.

Original languageAmerican English
Article number9
JournalFrontiers in Chemistry
Issue numberMAR
StatePublished - 2014

Bibliographical note

Publisher Copyright:
© 2014 Gabizon and Friedler.


  • Allostery
  • Drug design
  • HIV-1
  • Peptides
  • Protein oligomerization
  • Shiftides


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