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Cited by 261

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Adsorption of Proteins to Hydrophobic Sites on Mixed Self-Assembled Monolayers

Ostuni, Emanuele, Grzybowski, Bartosz A., Mrksich, Milan, Roberts, Carmichael S., Whitesides, George M.·2003·Langmuir
DOI 10.1021/la020649c
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Abstract

This paper describes a technique that uses mixed self-assembled monolayers of two alkanethiolates ( - S(CH 2 ) 11 (OCH 2 CH 2 ) 6 OR, R = a hydrophobic group, and - S(CH 2 ) 11 (OCH 2 CH 2 ) n OH, n = 3, 6, EG n OH), 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(C 6 H 5 ) 3, CH(C 6 H 5 ) 2, and CH 2 (C 6 H 5 ). 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.

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Metadata

Authors
Ostuni, E., Grzybowski, B. A., Mrksich, M., Roberts, C. S., & Whitesides, G. M.
Venue
Langmuir
Publisher
American Chemical Society (ACS)
Published
2003-01-17
Volume
19
Issue
5
Pages
1861-1872
ISSN
  • 0743-7463 (ISSN-L)
  • 1520-5827
DOI
10.1021/la020649c
OpenAlex
W2082912875
Cited by
261
References
32
FWCI
12.37
Type
journal article
Language
en
Open access
closed

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