Examining lysozyme structures on polyzwitterionic brush surfaces

Haoyu Wang, Pinar Akcora

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Conformational structures of lysozyme at the interfaces of hydrophilic polymer poly[2-(methacryloyloxy)ethyl dimethyl-(3-sulfopropyl)ammonium hydroxide] (PMEDSAH), are examined to understand the role of protein-polymer interactions on the stability of lysozyme. This work underpins the effect of hydration layer on the structures of physically adsorbed lysozyme on PMEDSAH brushes. Hydrophilic nature and strength of hydration layers around brushes are controlled by varying the brush thickness and temperature. We measured that lysozyme is structurally less stable on 15 nm thick hydrophilic PMEDSAH brushes at 75 °C than at room temperature. To the contrary, 5–8 nm thick brushes stretch in hydrated state by heating, hence yield higher structural stability of lysozyme. These results suggest that short polyzwitterionic brushes can facilitate improved biomaterial interactions that are essential for biosensors performing at elevated temperatures.

Original languageEnglish
Pages (from-to)215-219
Number of pages5
JournalColloids and Surfaces B: Biointerfaces
Volume160
DOIs
StatePublished - 1 Dec 2017

Keywords

  • Biointerface
  • Hydration layer
  • Lysozyme
  • PMEDSAH
  • Polyzwitterionic brush
  • Protein structure
  • Stability

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