Self-assembled monolayers of methyl 1-thiahexa(ethylene oxide) for the inhibition of protein adsorption

Langmuir

Volumn 18, Issue 12, 2002, Pages 4674-4680

  Vanderah, David J ^a   Valincius, Gintaras ^a,b   Meuse, Curtis W ^a  

^a NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

^b VILNIUS UNIVERSITY   (Lithuania)

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION SPECTROSCOPY; ADSORPTION; CAPACITANCE; CONFORMATIONS; CRYSTAL DEFECTS; ELECTROCHEMISTRY; ETHANOL; INFRARED SPECTROSCOPY; MOLECULAR STRUCTURE; SELF ASSEMBLY; SOLUTIONS;

HELICAL STRUCTURES;

PROTEINS;

EID: 0037062793     PISSN: 07437463     EISSN: None     Source Type: Journal    
DOI: 10.1021/la025720t     Document Type: Article

References (41)

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25. The specification of commercial products is for clarity only and does not constitute endorsement by NIST.
26. IUPAC name: 3,6,9,12,15,18-hexaoxanonadecanethiol.
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32. 2O- unit (0.278 nm)]}. The S-Au bond distance from: Sellers, H.; Ulman, A.; Shnidman, Y.; Eilers, J.E. J. Am. Chem. Soc. 1993, 115, 9389-9401. All-trans extended conformation = 2.49 nm {2.14 (6 × 0.356 nm (ref 11)) + 0.04 nm (C-S bond length differential relative to C-O bond length) + 0.19 nm (Au-S bond length) + 0.12 nm (1/3 of 0.356 nm)}.
33. 2O- unit (0.278 nm)]}. The S-Au bond distance from: Sellers, H.; Ulman, A.; Shnidman, Y.; Eilers, J.E. J. Am. Chem. Soc. 1993, 115, 9389-9401. All-trans extended conformation = 2.49 nm {2.14 (6 × 0.356 nm (ref 11)) + 0.04 nm (C-S bond length differential relative to C-O bond length) + 0.19 nm (Au-S bond length) + 0.12 nm (1/3 of 0.356 nm)}.
34. 2 bands.
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36. fibrinogen (∼0.002 au) ≈ 60% of a protein monolayer], assuming all adsorbed proteins are essentially undenatured. The latter assumption is supported by near identical relative intensities of the BSA and lysozyme amide I/amide II bands (2/1) to those for fibrinogen (ref 11) and the known low denaturation of proteins on OEO chains (see: Yang, Z.; Galloway, J.A.; Yu, H. Langmuir 1999, 15, 8405). The ∼50% coverage is further supported by the nearly 2 times absorbance of the amide I and amide II bands after 24 h [∼0.006 au and ∼0.003 au, respectively (data not shown)], from which a full protein monolayer is likely.
37. The lower detectable limit is estimated at 2-3% of a protein monolayer.
38. Vanderah, D.J.; Gates, R.S.; Silin, V.; Meuse, C.W.; Zeiger, D.N.; Valincius, G. Langmuir, submitted.
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40. Our preliminary data suggesting protein-induced conformational changes in the SAMs are consistent with earlier data (ref 11) but will require a more systematic study to determine the validity of this hypothesis and to define the scope and magnitude of such effects.
41. Morra, M. J. Biomater. Sci., Polym. Ed. 2000, 11, 547-569.