Control of protein-ligand recognition using a stimuli-responsive polymer.

Journal Article (Journal Article)

Stimuli-responsive polymers exhibit reversible phase changes in response to changes in environmental factors such as pH or temperature. Conjugating such polymers to antibodies and proteins provides molecular systems for applications such as affinity separations, immunoassays and enzyme recovery and recycling. Here we show that conjugating a temperature-sensitive polymer to a genetically engineered site on a protein allows the protein's ligand binding affinity to be controlled. We synthesized a mutant of the protein streptavidin to enable site-specific conjugation of the responsive polymer near the protein's binding site. Normal binding of biotin to the modified protein occurs below 32 degrees C, whereas above this temperature the polymer collapses and blocks binding. The collapse of the polymer and thus the enabling and disabling of binding, is reversible. Such environmentally triggered control of binding may find many applications in biotechnology and biomedicine, such as the control of enzyme reaction rates and of biosensor activity, and the controlled release of drugs.

Full Text

Duke Authors

Cited Authors

  • Stayton, PS; Shimoboji, T; Long, C; Chilkoti, A; Chen, G; Harris, JM; Hoffman, AS

Published Date

  • November 1995

Published In

Volume / Issue

  • 378 / 6556

Start / End Page

  • 472 - 474

PubMed ID

  • 7477401

Electronic International Standard Serial Number (EISSN)

  • 1476-4687

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/378472a0


  • eng