Probing Single Biomolecules with Atomic Force Microscopy

Fritz, Jürgen; Anselmetti, Dario; Jarchow, Janina; Fernàndez‐Busquets, Xavier

doi:10.1006/jsbi.1997.3887

Cited by 75 publications

(68 citation statements)

References 32 publications

(34 reference statements)

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“…Our findings, as well as those of others, 27,28,30,64,65 clearly show that AFM has more than sufficient sensitivity to detect the height increase that occurs from the formation of a single antibody-antigen pair. Thus, the issue of adequate sensitivity has been addressed.…”

Section: Discussionsupporting

confidence: 86%

Microminiaturized Immunoassays Using Atomic Force Microscopy and Compositionally Patterned Antigen Arrays

Jones¹,

Kenseth²,

Porter³

et al. 1998

Anal. Chem.

132

119

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This paper combines the topographic imaging capability of the atomic force microscope (AFM) with a compositionally patterned array of immobilized antigenic rabbit IgG on gold as an approach to performing immunoassays. The substrates are composed of micrometer-sized domains of IgG that are covalently linked to a photolithographically patterned array of a monolayer-based coupling agent. The immobilized coupling agent, which is prepared by the chemisorption of dithiobis(succinimidyl undecanoate) on gold, is separated by micrometer-sized grids of a monolayer formed from octadecanethiol (ODT). The strong hydrophobicity of the ODT adlayer, combined with the addition of the surfactant Tween 80 to the buffer solution that is used in forming the antibody-antigen pairs, minimizes the nonspecific adsorption of proteinaceous materials to the grid regions. This minimization allows the grids to function as a reference plane for the AFM detection of the height increase when a complementary antibody-antigen pair is formed. The advantageous features of this strategy, which include ease of sample preparation, an internal reference plane for the detection of topographic changes, and the potential for regeneration and reuse, are demonstrated using rabbit IgG as an immobilized antigen and goat anti-rabbit IgG as the complementary antibody. The prospects for further miniaturization are discussed.Immunoassays play a critical role in clinical, pharmaceutical, and environmental chemistries. [1][2][3] To such ends, a range of different transduction (e.g., optical, 4-6 amperometric, 7 radiochemical, 8 piezoelectric, 9-13 and capacitive 14,15 ) mechanisms have been successfully exploited for the detection of antigen-antibody binding. However, radiochemical, amperometric, and optical

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Section: Discussionsupporting

confidence: 86%

Microminiaturized Immunoassays Using Atomic Force Microscopy and Compositionally Patterned Antigen Arrays

Jones¹,

Kenseth²,

Porter³

et al. 1998

Anal. Chem.

132

119

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“…Individual CVD nanotube tips routinely show higher-resolution images of isolated protein molecules than our previous results with MWNT and SWNT bundle tips (consistent with measurements on gold nanoclusters) and room-temperature AFM data with commercial tips 12 , and are comparable to the high-resolution data obtained at low temperatures by cryo-AFM 13 . Our results reflect the small radii, cylindrical shape and low adhesion forces (typically less than 30 pN) of individual MWNT tips.…”

supporting

confidence: 87%

Growth of nanotubes for probe microscopy tips

Hafner

Cheung

Lieber

1999

Nature

383

228

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“…[24,1046]). Two main fields of interest have emerged in recent years: Molecule stretching [1047][1048][1049] and specific interactions between biological pairs [1050][1051][1052]. Accordingly, two relevant classes of models have been developed: One to describe the stretching of a linear polymer, the other to describe rupture of a single bond.…”

Section: Single Moleculesmentioning

confidence: 99%