Adsorption of proteins to hydrophobic sites on mixed self-assembled monolayers

Emanuele Ostuni, Bartosz A. Grzybowski, Milan Mrksich, Carmichael S. Roberts, George M. Whitesides*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

216 Scopus citations

Abstract

This paper describes a technique that uses mixed self-assembled monolayers of two alkanethiolates (-S(CH2)11(OCH2CH2)6 OR, R = a hydrophobic group, and -S(CH2)11(OCH2CH2)n OH, n = 3, 6, EGnOH), in combination with surface plasmon resonance spectroscopy, to study the influence of the size and shape of R, and its density at the surface, on the hydrophobic adsorption of proteins at solid - liquid interfaces. Detailed results were obtained for β-galactosidase, carbonic anhydrase, lysozyme, and RNase A using R = C(C6H5)3, CH(C6H5)2, and CH2(C6H5). A hard-sphere model is used to rationalize the adsorption; this model, although very approximate, helps to interpret qualitative trends in the data. Using this model, the extent to which adsorbed proteins undergo conformational rearrangements appears to depend on the density of the hydrophobic groups at the surface and on the concentration of protein in solution. This paper describes the first step toward the development of a system that will allow the study of hydrophobic interactions of proteins with surfaces presenting organic groups of well-defined shape.

Original languageEnglish (US)
Pages (from-to)1861-1872
Number of pages12
JournalLangmuir
Volume19
Issue number5
DOIs
StatePublished - Mar 4 2003

ASJC Scopus subject areas

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

Fingerprint Dive into the research topics of 'Adsorption of proteins to hydrophobic sites on mixed self-assembled monolayers'. Together they form a unique fingerprint.

Cite this