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

Article Abstract:

Conjugation of a temperature-sensitive polymer to a genetically engineered site on a protein helps in regulating the protein's ligand binding affinity. A study of a mutant of the protein streptavidin indicates that the binding of biotin to the mutant is normal below 32 degrees celsius, but the polymer collapses and inhibits binding above that temperature. The mutant has a polymer conjugation domain close to the outer edge of the biotin-binding pocket. Environmentally induced control of binding has various biological applications.

Usage, Polymers, Genetic engineering, Protein binding, Thermal properties

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Graft copolymers that exhibit temperature-induced phase transitions over a wide range of pH

Article Abstract:

A newly developed 'intelligent' aqueous polymer system exhibits characteristic solubility variations in water in response to the changes in temperature and hydrogen ion concentration (pH). The grafting of temperature-sensitive side chains onto a pH-sensitive backbone results in the formation of the polymer, which can be used in biotechnology, industry, medicine and environmental pollution control.

Phase transformations (Statistical physics), Phase transitions (Physics), Graft copolymers

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Size-dependent control of the binding of biotinylated proteins to streptavidin using a polymer shield

Article Abstract:

Research into the binding of stimuli-responsive polymers to proteins is described. By using a polymer shield to bind biotinylated proteins to the protein streptavidin, it is shown that size-selective binding of big, macromolecular ligands can be achieved.

Analysis, Proteins, Letter to the Editor, Protein research

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