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Cyclodextrin-hydrophobe complexation in associative polymers.

Shamsheer Mahammad1, George W Roberts1, Saad A Khan1

  • 1Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, USA. khan@eos.ncsu.edu groberts@ncsu.edu.

Soft Matter
|September 9, 2020
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Summary
This summary is machine-generated.

We developed a new rheology method to study cyclodextrins (CD) complexation with hydrophobes in polymer solutions. This method quantizes CD-hydrophobe binding, revealing β-CD has higher affinity than α-CD.

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Area of Science:

  • Polymer Science
  • Supramolecular Chemistry
  • Rheology

Background:

  • Associative polymers form transient networks via hydrophobic interactions, leading to solution thickening.
  • Cyclodextrins (CD) encapsulate hydrophobic groups, significantly reducing polymer solution viscoelasticity.

Purpose of the Study:

  • To develop a novel rheology-based method for studying cyclodextrin-hydrophobe complexation.
  • To establish a Langmuir-type adsorption isotherm for quantifying binding constants.
  • To investigate the thermodynamic parameters (enthalpy, entropy) of complexation.

Main Methods:

  • Rheological measurements of hydrophobically modified associative polymer solutions.
  • Addition of cyclodextrins (α- and β-CD) to observe changes in viscoelastic properties.
  • Development of a model correlating elastic modulus reduction to CD adsorption.

Main Results:

  • A rheology-based method was established to quantify cyclodextrin-hydrophobe binding.
  • β-Cyclodextrin exhibited a higher binding constant than α-cyclodextrin at equivalent conditions.
  • Thermodynamic analysis indicated that α-CD complexation results in greater enthalpy and entropy changes.

Conclusions:

  • The developed rheological method effectively probes molecular complexation in polymer solutions.
  • Binding affinity is influenced by cyclodextrin size, with smaller α-CD showing higher affinity due to a snugger fit.
  • Thermodynamic data provides insights into the driving forces of cyclodextrin-hydrophobe interactions.