Nanotechnological characterization of human serum albumin adsorption on wet synthetic polymer dialysis membrane surfaces

ASAIO J. 2009 May-Jun;55(3):236-42. doi: 10.1097/MAT.0b013e3181984229.

Abstract

The objective of the present study was to evaluate the characteristics of protein adsorption on the inner surface of various dialysis membranes, to develop protein adsorption-resistant biocompatible dialysis membranes. The adsorption force of human serum albumin (HSA) on the inner surface of a dialysis membrane and the smoothness of the membrane were evaluated from a nanoscale perspective by atomic force microscopy. The content ratio of the hydrophilic polymer, polyvinylpyrrolidone (PVP), was determined by attenuated total reflection Fourier transform infrared spectroscopy. Nine synthetic-polymer dialysis membranes on the market made of polysulfone (PSF), polyethersulfone (PES), polyester polymer-alloy (PEPA), and ethylene vinylalcohol (EVAL) were used in the present study. The HSA adsorption force on the surface of the hydrophobic polymer PEPA membrane was higher than that on the hydrophilic polymer EVAL membrane surface. It has been considered beneficial, for decreasing the HSA adsorption force, to cover a hydrophobic polymer membrane surface with PVP. However, there were some areas on PVP-containing membrane surfaces at which much higher HSA adsorption forces were observed. The HSA adsorption force gave a nearly linear correlation with the surface roughness on the PSF membrane surface. However, the HSA adsorption force was uncorrelated with the PVP content ratio for any of the PSF membrane surfaces tested. In conclusion, protein adsorption can be minimized by the use of dialysis membranes made of hydrophobic polymers containing PVP with a smooth surface.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Humans
  • Membranes, Artificial*
  • Nanotechnology
  • Renal Dialysis / instrumentation*
  • Serum Albumin / pharmacokinetics*
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Membranes, Artificial
  • Serum Albumin