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Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption

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Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption. / Dilly, Suzanne J.; Beecham, Matthew P.; Brown, Steven P. et al.
In: Langmuir, Vol. 22, No. 19, 12.09.2006, p. 8144-8150.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Dilly, SJ, Beecham, MP, Brown, SP, Griffin, JM, Clark, AJ, Griffin, CD, Marshall, J, Napier, RM, Taylor, PC & Marsh, A 2006, 'Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption', Langmuir, vol. 22, no. 19, pp. 8144-8150. https://doi.org/10.1021/la060743j

APA

Dilly, S. J., Beecham, M. P., Brown, S. P., Griffin, J. M., Clark, A. J., Griffin, C. D., Marshall, J., Napier, R. M., Taylor, P. C., & Marsh, A. (2006). Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption. Langmuir, 22(19), 8144-8150. https://doi.org/10.1021/la060743j

Vancouver

Dilly SJ, Beecham MP, Brown SP, Griffin JM, Clark AJ, Griffin CD et al. Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption. Langmuir. 2006 Sept 12;22(19):8144-8150. Epub 2006 Aug 9. doi: 10.1021/la060743j

Author

Dilly, Suzanne J. ; Beecham, Matthew P. ; Brown, Steven P. et al. / Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption. In: Langmuir. 2006 ; Vol. 22, No. 19. pp. 8144-8150.

Bibtex

@article{8601aa647ed1465d9ad2bd9174197d47,
title = "Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption",
abstract = "Novel surfaces derivatized with tertiary amine oxides have been prepared and tested for their ability to resist nonspecific protein adsorption. The oxidation of tertiary amines supported on triazine units was carried out using mCPBA to give a format allowing conjugation of biologically active ligands alongside them. Adsorption to these surfaces was tested and compared to adsorption to a set of commercial and custom oligo-/poly(ethylene glycol) (OEG/PEG) supports by challenging them with a protein display library presented on bacteriophage I. The new class of amine oxide surfaces is found to compare favorably with the performance of the OEG/PEG supports in the prevention of nonspecific binding.",
keywords = "SELF-ASSEMBLED MONOLAYERS, POLY(ETHYLENE GLYCOL), CROSS-POLARIZATION, GOLD, BIOMATERIALS, COSOLVENTS, STABILITY, DENSITY, NMR",
author = "Dilly, {Suzanne J.} and Beecham, {Matthew P.} and Brown, {Steven P.} and Griffin, {John M.} and Clark, {Andrew J.} and Griffin, {Craig D.} and Jacqueline Marshall and Napier, {Richard M.} and Taylor, {Paul C.} and Andrew Marsh",
year = "2006",
month = sep,
day = "12",
doi = "10.1021/la060743j",
language = "English",
volume = "22",
pages = "8144--8150",
journal = "Langmuir",
issn = "0743-7463",
publisher = "AMER CHEMICAL SOC",
number = "19",

}

RIS

TY - JOUR

T1 - Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption

AU - Dilly, Suzanne J.

AU - Beecham, Matthew P.

AU - Brown, Steven P.

AU - Griffin, John M.

AU - Clark, Andrew J.

AU - Griffin, Craig D.

AU - Marshall, Jacqueline

AU - Napier, Richard M.

AU - Taylor, Paul C.

AU - Marsh, Andrew

PY - 2006/9/12

Y1 - 2006/9/12

N2 - Novel surfaces derivatized with tertiary amine oxides have been prepared and tested for their ability to resist nonspecific protein adsorption. The oxidation of tertiary amines supported on triazine units was carried out using mCPBA to give a format allowing conjugation of biologically active ligands alongside them. Adsorption to these surfaces was tested and compared to adsorption to a set of commercial and custom oligo-/poly(ethylene glycol) (OEG/PEG) supports by challenging them with a protein display library presented on bacteriophage I. The new class of amine oxide surfaces is found to compare favorably with the performance of the OEG/PEG supports in the prevention of nonspecific binding.

AB - Novel surfaces derivatized with tertiary amine oxides have been prepared and tested for their ability to resist nonspecific protein adsorption. The oxidation of tertiary amines supported on triazine units was carried out using mCPBA to give a format allowing conjugation of biologically active ligands alongside them. Adsorption to these surfaces was tested and compared to adsorption to a set of commercial and custom oligo-/poly(ethylene glycol) (OEG/PEG) supports by challenging them with a protein display library presented on bacteriophage I. The new class of amine oxide surfaces is found to compare favorably with the performance of the OEG/PEG supports in the prevention of nonspecific binding.

KW - SELF-ASSEMBLED MONOLAYERS

KW - POLY(ETHYLENE GLYCOL)

KW - CROSS-POLARIZATION

KW - GOLD

KW - BIOMATERIALS

KW - COSOLVENTS

KW - STABILITY

KW - DENSITY

KW - NMR

U2 - 10.1021/la060743j

DO - 10.1021/la060743j

M3 - Journal article

VL - 22

SP - 8144

EP - 8150

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 19

ER -