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5621343 
Journal Article 
Control of protein-ligand recognition using a stimuli-responsive polymer 
Stayton, PS; Shimoboji, T; Long, C; Chilkoti, A; Chen, G; Harris, JM; Hoffman, AS 
1995 
1 
Nature
ISSN: 0028-0836
EISSN: 1476-4687 
Nature. 
378 
6556 
472-4. [Nature] 
English 
7477401 
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. 
Acrylic Resins/metabolism; Bacterial Proteins/genetics/metabolism; Biotin/metabolism; Cysteine/metabolism; Cytochromes b5/metabolism; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Polymers/metabolism; Protein Binding; Protein Conformation; Recombinant Proteins/genetics/metabolism; Streptavidin; Sulfones/metabolism; Temperature; 25189-55-3; 5PFN71LP8M; 6SO6U10H04; 9013-20-1; 9035-39-6; K848JZ4886