Proteomic Characterization of a New asymmetric Cellulose Triacetate Membrane for Hemodialysis

Maurizio Ronci, Lidia Leporini, Paolo Felaco, Vittorio Sirolli, Luisa Pieroni, Viviana Greco, Antonio Aceto, Andrea Urbani, Mario Bonomini

Risultato della ricerca: Contributo in rivistaArticolo in rivista

6 Citazioni (Scopus)


Purpose: The artificial membrane inside the haemodialyzer is the main determinant of the quality and success of haemodialysis therapy. The performances of haemodialysis membranes are highly influenced by the interactions with plasma proteins, which in turn are related to the physical and chemical characteristics of the membrane material. The present cross-over study is aimed to analyse the haemodialysis performance of a newly developed asymmetric cellulose triacetate membrane (ATA) in comparison to the conventional parent symmetric polymer (CTA). Experimental design: In four chronic non diabetic haemodialysis patients, the protein constituents of the adsorbed material from the filters after the haemodialysis session, and the proteins recovered in the ultrafiltrate during the session, are identified using a bottom-up shotgun proteomics approach. Results: The ATA membrane shows a lower protein adsorption rate and a lower mass distribution pattern of the proteinaceous material. Conclusions and clinical relevance: By highlighting the differences between the two haemodialysis filters in terms of adsorbed proteins and flow through, it is demonstrated the higher biocompatibility of the novel ATA membrane, that fulfils the indications for the development of more performant membranes and may represent a step forward for the treatment of patients on chronic haemodialysis.
Lingua originaleEnglish
pagine (da-a)N/A-N/A
Stato di pubblicazionePubblicato - 2018


  • Adolescent
  • Adsorption
  • Adult
  • Blood Proteins
  • Cellulose
  • Cross-Over Studies
  • Female
  • Humans
  • Male
  • Membranes, Artificial
  • Polymers
  • Proteomics
  • Renal Dialysis
  • Young Adult
  • liquid chromatography tandem mass spectrometry
  • protein identification


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