Hydrogel microspheres III. Temperature-dependent adsorption of proteins on poly-N-isopropylacrylamide hydrogel microspheres

Haruma Kawaguchi, Keiji Fujimoto, Yoshiro Mizuhara

Research output: Contribution to journalArticle

290 Citations (Scopus)

Abstract

Precipitation polymerization of N-isopropylacrylamide (NIPAM) with methylenebisacrylamide (MBAAm) in water at 70°C gave thermosensitive hydrogel microspheres. The adsorbability of proteins on the poly-NIPAM microspheres was found to depend on temperature. Below the lower critical solution temperature (LCST) of poly-NIPAM in an aqueous medium, that is, around 32°C, the microspheres hold a large amount of water inside and their surface is hydrophilic enough to suppress the adsorption of proteins. On the contrary, above 32°C, the micropheres deswell and their surface becomes hydrophobic and, consequently, susceptible to adsorption of a large amount of proteins. Proteins once adsorbed on the microspheres at a high temperature could be desorbed more or less by lowering the temperature to below 32°C. The extent of desorption at low temperatures was found to depend on the incubation time for adsorption at high temperatures.

Original languageEnglish
Pages (from-to)53-57
Number of pages5
JournalColloid & Polymer Science
Volume270
Issue number1
DOIs
Publication statusPublished - 1992 Jan

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Keywords

  • adsorption and desorption
  • Hydrogel
  • hydrophilicity
  • microsphere
  • protein
  • thermosensitivity

ASJC Scopus subject areas

  • Polymers and Plastics
  • Materials Chemistry
  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

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