Differential regulation of protein subdomain activity with caged bivalent ligands

Chembiochem. 2009 Mar 2;10(4):654-7. doi: 10.1002/cbic.200800814.

Abstract

Subtle change: Spatiotemporal modulation of individual protein subdomains with light as the trigger signal becomes possible by using bivalent aptamers and introducing photolabile "caging groups" to switch individual aptamer modules ON or OFF differentially. To the best of our knowledge, this is the first study to show that it is possible to modulate individual domain activity in aptamers, and thus also domain activity in proteins, with light.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aptamers, Nucleotide / chemistry*
  • Aptamers, Nucleotide / genetics
  • Aptamers, Nucleotide / pharmacology*
  • Ligands
  • Mutation
  • Nucleosides / chemistry
  • Protein Structure, Tertiary
  • Proteins / antagonists & inhibitors
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Thrombin / antagonists & inhibitors
  • Thrombin / chemistry
  • Thrombin / metabolism

Substances

  • Aptamers, Nucleotide
  • Ligands
  • Nucleosides
  • Proteins
  • Thrombin