Affinity of Serum Albumin and Fibrinogen to Cellulose, Its Hydrophobic Derivatives and Blends

Rupert Kargl*, Matej Bračič, Matic Resnik, Miran Mozetič, Wolfgang Bauer, Karin Stana Kleinschek, Tamilselvan Mohan

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

This work describes the preparation of spin-coated thin polymer films composed of cellulose (CE), ethyl cellulose (EC), and cellulose acetate (CA) in the form of bi- or mono-component coatings on sensors of a quartz crystal microbalance with dissipation monitoring (QCM-D). Depending on the composition and derivative, hydrophilicity can be varied resulting in materials with different surface properties. The surfaces of mono- and bi-component films were also analyzed by atomic force microscopy (AFM) and large differences in the morphologies were found comprising nano- to micrometer sized pores. Extended protein adsorption studies were performed by a QCM-D with 0.1 and 10 mg mL−1 bovine serum albumin (BSA) and 0.1 and 1 mg mL−1 fibrinogen from bovine plasma in phosphate buffered saline. Analysis of the mass of bound proteins was conducted by applying the Voigt model and a comparison was made with the Sauerbrey wet mass of the proteins for all films. The amount of deposited proteins could be influenced by the composition of the films. It is proposed that the observed effects can be exploited in biomaterial science and that they can be used to extent the applicability of bio-based polymer thin films composed of commercial cellulose derivatives.

Original languageEnglish
Article number581
JournalFrontiers in Chemistry
Volume7
DOIs
Publication statusPublished - 6 Sept 2019

Keywords

  • albumin
  • cellulose acetate
  • ethyl cellulose
  • fibrinogen
  • hydrophilicity
  • protein adsorption
  • quartz crystal microbalance

ASJC Scopus subject areas

  • General Chemistry

Fingerprint

Dive into the research topics of 'Affinity of Serum Albumin and Fibrinogen to Cellulose, Its Hydrophobic Derivatives and Blends'. Together they form a unique fingerprint.

Cite this