Related Experiment Video
Updated: Apr 30, 2026

Controlled Synthesis and Fluorescence Tracking of Highly Uniform PolyN-isopropylacrylamide Microgels
Published on: September 8, 2016
Interaction of poly(N-isopropylacrylamide) with sodium dodecyl sulfate below the critical aggregation concentration
1Graduate School of Engineering, Utsunomiya University , 7-1-2 Yoto, Utsunomiya, Tochigi 321-8585, Japan.
Abstract:
Interaction between the thermoresponsive polymer poly(N-isopropylacrylamide) (P-NIP) and sodium dodecyl sulfate (SDS) both above and below its phase transition temperature was examined under dilute conditions. Above the lower critical solution temperature (LCST) of P-NIP (32 °C), 0.01 wt % P-NIP specifically interacted with 1.0 × 10(-5) mol/L SDS to form a precipitate. However, when SDS was added at concentrations above or below 1.0 × 10(-5) mol/L, the P-NIP solution remained clear above the LCST. A fluorometric probe, N-phenyl-naphthalene, indicated that the hydrophobicity of the aggregates composed of P-NIP and SDS changed at an SDS concentration of 1.0 × 10(-5) mol/L. Although the hydrophobicity of the precipitate was similar to that of P-NIP alone at less than 1.0 × 10(-5) mol/L, it approached that of SDS homomicelles as the SDS concentration increased above 1.0 × 10(-5) mol/L. Dynamic light scattering and turbidimetry studies showed no P-NIP phase transition above an SDS concentration of 1.0 × 10(-5) mol/L, which is much lower than the reported critical association concentration (CAC) of SDS with P-NIP. This indicates that P-NIP interacted with SDS above the LSCT at much lower SDS concentration than the reported CAC.
Related Concept Videos
Micelles
SDS-PAGE
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact...
Detergent Purification of Membrane Proteins

