A scanning force microscopy study of human serum albumin and porcine pancreas trypsin adsorption on mica surfaces

Quist, Arjan P.; Björck, Lars; Reimann, C.T.; Oscarsson, Sven; Sundqvist, B.

doi:10.1016/0039-6028(94)00809-4

Cited by 47 publications

(48 citation statements)

References 25 publications

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“…The height for the resulting rabbit IgG adlayer in the squares is 3-4 nm larger than the ODT adlayer in the grids. Importantly, this range of height increase is in reasonable agreement with previously reported findings, [27][28][29][30][31]60 indicating the successful creation of a patterned array of antibodies. The differences in friction are also consistent with the expected differences in the composition of the two components for the patterned surface.…”

Section: Resultssupporting

confidence: 92%

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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: Resultssupporting

confidence: 92%

“…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: 85%

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 average height is smaller than the height of a single HSA molecule in solution, which was reported to be ≈3-8 nm based on X-ray diffraction studies. [6] In the ex situ AFM study of Quist et al, [7] the average height of individual HSA molecules adsorbed on mica was (0.60 ± 0.12) nm, the average width was (22.9 ± 2.9) nm. The dimensions found in the present investigation are in line with the results in literature.…”

Section: Afmmentioning

confidence: 95%

“…The adsorption of HSA has been investigated in the past ex situ by means of AFM on different model surfaces, including mica, [7] graphite [8] and self-assembled monolayer surfaces. [9] The major disadvantage is that these model substrates are not used as such in implants.…”

Section: Introductionmentioning

confidence: 99%

The interaction of human serum albumin with titanium studied by means of atomic force microscopy

Keere

Willaert

Tourwe

et al. 2008

Surface & Interface Analysis

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a Titanium is frequently used as a biomaterial for implants in orthopaedics and cardiovascular devices. Understanding the biocompatibility, which is strongly influenced by the adsorption of proteins onto the surface, is very important to improve implants. The surface chemistry of an implant material and its influence on the interaction with body fluid is crucial in that perspective. The main goal of this study was to investigate the conformation of human serum albumin (HSA) with commercially pure titanium (CP Ti) on a molecular level. Both ex situ and in situ AFM imaging showed the conformation of HSA on CP Ti and on mica, which was used as a reference material. Single molecules and aggregates of albumin were observed. HSA can be recognised by the globular shape. The conformation of the adsorbed HSA molecules was different on titanium and mica, for both the ex situ and in situ imaging. The difference in wettability between both substrates caused a larger spread of the protein on the CP Ti surface and thus resulted in a larger perturbation of the native structure of HSA as compared to mica.

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“…[20][21][22][23] . The potential of the AFM to image single molecules under mild conditions makes it possible to investigate the structure/conformation of adsorbed proteins 24 at high resolution and on various surfaces; one example is human plasma fibrinogen. 25,26 In this study, AFM has been used in ambient and liquid conditions at low ionic strength to assess the influence of the surface on the structure of human plasma Fn when adsorbed to silica, mica, and methylated (hydrophobic) silica surfaces, three surfaces with different physical properties.…”

Section: Introductionmentioning

confidence: 99%

Surface‐dependent conformations of human plasma fibronectin adsorbed to silica, mica, and hydrophobic surfaces, studied with use of Atomic Force Microscopy

Bergkvist

Carlsson

Oscarsson

2002

J Biomedical Materials Res

210

255

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Human plasma fibronectin (Fn) is a large flexible protein stabilized by intermolecular ionic interactions forming a compact structure. On altering solution conditions, the structure can revert to a more expanded state, thereby exposing previously hidden domains (e.g., cell-binding sites). Electron microscopy images of Fn air-sprayed onto mica surfaces show elongated protein structures, indicating a surface-induced structural change. This makes it interesting to investigate the influence of surface properties on the structure of adsorbed Fn. We have used intermittent-contact Atomic Force Microscopy to investigate the structure of Fn adsorbed onto mica, silica, and methylated silica surfaces. We observed that on silica surfaces, which is hydrophilic, most (70%) of the molecules had an elongated structure with partial intramolecular chain interactions, compare to molecules adsorbed on hydrophobic, methylated surfaces, where a compact structure predominated (70%). On mica surfaces, both compact and elongated protein structures were observed, with a slight preference for the elongated form (53%). Results show that surface physical properties influence the molecular structure of fibronectin on adsorption, which could provide useful information in understanding surface-induced in vivo responses.

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A scanning force microscopy study of human serum albumin and porcine pancreas trypsin adsorption on mica surfaces

Cited by 47 publications

References 25 publications

Microminiaturized Immunoassays Using Atomic Force Microscopy and Compositionally Patterned Antigen Arrays

Microminiaturized Immunoassays Using Atomic Force Microscopy and Compositionally Patterned Antigen Arrays

The interaction of human serum albumin with titanium studied by means of atomic force microscopy

Surface‐dependent conformations of human plasma fibronectin adsorbed to silica, mica, and hydrophobic surfaces, studied with use of Atomic Force Microscopy

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