Peptide fibrils as monomer storage of the covalent HIV-1 integrase inhibitor

Koushik Chandra, Priyadip Das, Norman Metanis, Assaf Friedler, Meital Reches*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


We have recently reported the covalent inhibition of HIV-1 integrase by an N-terminal succinimide-modified lens epithelium-derived growth factor (361–370) peptide. We also showed that this peptide is proteolytically stable. Here, we show that this inhibitor is stored as fibrils that serve as a stock for the inhibitory monomers. The fibrils increase the local concentration of the peptide at the target protein. When the monomers bind integrase, the equilibrium between the fibrils and their monomers shifts towards the formation of peptide monomers. The combination of fibril formation and subsequent proteolytic stability of the peptide may bring to new strategy for developing therapeutic agents.

Original languageAmerican English
Pages (from-to)117-121
Number of pages5
JournalJournal of Peptide Science
Issue number2
StatePublished - 1 Feb 2017

Bibliographical note

Publisher Copyright:
Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.


  • HIV-1 integrase
  • covalent inhibition
  • fibrillization
  • peptides
  • succinimide


Dive into the research topics of 'Peptide fibrils as monomer storage of the covalent HIV-1 integrase inhibitor'. Together they form a unique fingerprint.

Cite this