125I-radiolabeling, surface plasmon resonance, and quartz crystal microbalance with dissipation: Three tools to compare protein adsorption on surfaces of different wettability

Yafei Luan, Dan Li, Yanwei Wang, Xiaoli Liu, John L. Brash, Hong Chen

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The extent of protein adsorption is an important consideration in the biocompatibility of biomaterials. Various experimental methods can be used to determine the quantity of protein adsorbed, but the results usually differ. In the present work, self-assembled monolayers (SAMs) were used to prepare a series of model gold surfaces varying systematically in water wettability, from hydrophilic to hydrophobic. Three commonly used methods, namely, surface plasmon resonance (SPR), quartz crystal microbalance with dissipation (QCM-D), and 125I-radiolabeling, were employed to quantify fibrinogen (Fg) adsorption on these surfaces. This approach allows a direct comparison of the mass of Fg adsorbed using these three techniques. The results from all three methods showed that protein adsorption increases with increasing surface hydrophobicity. The increase in the mass of Fg adsorbed with increasing surface hydrophobicity in the SPR data was parallel to that from 125I- radiolabeling, but the absolute values were different and there does not seem to be a "universally congruent" relationship between the two methods for surfaces with varying wettability. For QCM-D, the variation in protein adsorption with wettability was different from that for SPR and radiolabeling. On the more hydrophobic surfaces, QCM-D gave an adsorbed mass much higher than from the two other methods, possibly because QCM-D measures both the adsorbed Fg and its associated water. However, on the more hydrophilic surfaces, the adsorbed mass from QCM-D was slightly greater than that from SPR, and both were smaller than from 125I-radiolabeling; this was true no matter whether the Sauerbrey equation or the Voigt model was used to convert QCM-D data to adsorbed mass.

Original languageEnglish
Pages (from-to)1029-1035
Number of pages7
JournalLangmuir
Volume30
Issue number4
DOIs
Publication statusPublished - Feb 4 2014

Fingerprint

Quartz crystal microbalances
Surface plasmon resonance
wettability
quartz crystals
surface plasmon resonance
microbalances
Wetting
dissipation
fibrinogen
proteins
Proteins
Adsorption
adsorption
Fibrinogen
Hydrophobicity
hydrophobicity
Water
Biocompatible Materials
Self assembled monolayers
biocompatibility

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

Cite this

125I-radiolabeling, surface plasmon resonance, and quartz crystal microbalance with dissipation : Three tools to compare protein adsorption on surfaces of different wettability. / Luan, Yafei; Li, Dan; Wang, Yanwei; Liu, Xiaoli; Brash, John L.; Chen, Hong.

In: Langmuir, Vol. 30, No. 4, 04.02.2014, p. 1029-1035.

Research output: Contribution to journalArticle

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