Creating “Smart” Surfaces Using Stimuli Responsive Polymers

TLDR

Surfaces modified with stimuli‑responsive polymers can dynamically alter their physico‑chemical properties in response to environmental changes, offering potential in biomaterials, biosensors, and microfluidic devices. The article reviews recent work and presents two laboratory examples of stimuli‑responsive surfaces. The authors describe a gold‑nanoparticle colorimetric assay to quantify SRP LCST behavior and a thermodynamically reversible addressing of proteins (TRAP) technique that uses ELP phase transition to modulate protein binding. The assay provides a simple, convenient method to assess SRP LCST behavior, while TRAP demonstrates reversible, spatio‑temporal control of protein binding at solid–liquid interfaces, opening avenues for new bioanalytical applications.

Abstract

Surfaces modified with stimuli-responsive polymers (SRPs) dynamically alter their physico-chemical properties in response to changes in their environmental conditions. The triggered control of interfacial properties provided by immobilized SRPs at the solid–water interface has application in the design of biomaterials, regenerable biosensors, and microfluidic bioanalytical devices. In this article, we briefly summarize recent research in this area, followed by two recent examples of research from our laboratory on stimuli-responsive surfaces. First, we present a new assay to quantify the phase transition behavior of SRPs at the solid–water interface. This assay, which is based on the distance-dependent colorimetric properties of gold nanoparticles, provides a technically simple and convenient method to determine the effect of different variables on the lower critical solution temperature (LCST) behavior of SRPs at the solid–water interface. Second, we show that stimuli-responsive surfaces can be created by the immobilization of an elastin-like polypeptide (ELP), a thermally responsive biopolymer, on a glass surface. We exploit the phase transition of the ELP at a surface to reversibly address an ELP fusion protein to a surface. This method, which we term thermodynamically reversible addressing of proteins (TRAP), enables the reversible, spatio-temporal modulation of protein binding at the solid-liquid interface, and will enable the realization of new bioanalytical applications.