文摘
Protein-adsorptive properties are a key feature of membranes used for hemodialysis treatment. Proteinadsorption is vital to the biocompatibility of a membrane material and influences membrane'sperformance. The object of the present study is to investigate membrane biocompatibility by correlatingthe adsorbed proteome repertoire with structural feature of the membrane surfaces. Minidialyzers ofidentical structural characteristics composed of either cellulose diacetate or ethylenevinyl alcoholmaterials were employed to develop an ex vivo apparatus to investigate protein adsorption. Adsorbedproteins were eluted by a strong chaotropic buffer condition and investigated by 2-DE coupled to bothMALDI-TOF mass spectrometry (MS) mass fingerprinting and fragmentation analysis on a nanoLC-MS/MS hybrid instrument. Membrane surface characterization included evaluation of roughness (atomicforce microscopy), elemental chemical composition (X-ray-photoelectron-spectroscopy), and hydrophilicity (pulsed nuclear magnetic resonance). The present study identifies a number of different proteinsas common or characteristic of filter material interaction, showing that proteomic techniques are apromising approach for the investigation of proteins surface-adsorbed onto hemodialysis membrane.Proteomic analysis enables the characterization of protein layers of unknown composition.