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Betulin-Constituted Multiblock Amphiphiles for Broad-Spectrum Protein Resistance.

Ye ChenQilei SongJunpeng ZhaoXiangjun GongHelmut SchlaadGuangzhao Zhang
Published in: ACS applied materials & interfaces (2018)
Multiblock-like amphiphilic polyurethanes constituted by poly(ethylene oxide) and biosourced betulin are designed for antifouling and synthesized by a convenient organocatalytic route comprising tandem chain-growth and step-growth polymerizations. The doping density of betulin (DB) in the polymer chain structure is readily varied by a mixed-initiator strategy. The spin-coated polymer films exhibit unique nanophase separation and protein resistance behaviors. Higher DB leads to enhanced surface hydrophobicity and, unexpectedly, improved protein resistance. It is found that the surface holds molecular-level heterogeneity when DB is substantially high due to restricted phase separation; therefore, broad-spectrum protein resistance is achieved despite considerable surface hydrophobicity. As DB decreases, the distance between adjacent betulin units increases so that hydrophobic nanodomains are formed, which provide enough landing areas for relatively small-sized proteins to adsorb on the surface.
Keyphrases
  • protein protein
  • amino acid
  • binding protein
  • ionic liquid
  • aqueous solution