Surface Plasmon Resonance Permits in Situ Measurement of Protein Adsorption on Self-Assembled Monolayers of Alkanethiolates on Gold

Milan Mrksich, George B. Sigal, George M. Whitesides*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

324 Scopus citations

Abstract

This paper demonstrates that surface plasmon resonance (SPR) spectroscopy can be used to measure the nonspecific adsorption of proteins to self-assembled monolayers (SAMs) of alkanethiolates on gold in situ and in real time. Mixed SAMs comprising hexa(ethylene glycol) and methyl groups that have values of χMe < 0.5 resisted the adsorption of four test proteins: RNase A, lysozyme, fibrinogen, and pyruvate kinase. These four proteins adsorbed irreversibly to surfaces having values of χMe > 0.5: the amount of adsorbed protein correlated with χMe- The initial rate for adsorption of fibrinogen to a methyl-terminated SAM (χMe = 1.0) followed first-order kinetics. The combination of SAMs and SPR described here is particularly well suited for investigations of the interactions of proteins with structurally well-defined organic surfaces.

Original languageEnglish (US)
Pages (from-to)4383-4385
Number of pages3
JournalLangmuir
Volume11
Issue number11
DOIs
StatePublished - Nov 1 1995

ASJC Scopus subject areas

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

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