Analysis of a non-labeling protein array on biotin modified gold surfaces using atomic force microscopy and surface plasmon resonance

Kim, Hyun‐Sook; Cho, Il-Hoon; Park, Jun Hyung; Kim, Somin; Paek, Se‐Hwan; Noh, Jaegeun; Lee, Haiwon

doi:10.1016/j.colsurfa.2007.04.155

Cited by 16 publications

(7 citation statements)

References 20 publications

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“…Well-ordered protein layers have great implications in biosensors [ 1 - 3 ], biomaterials [ 4 , 5 ] and protein-based molecular recognition at single-molecule scale [ 6 - 8 ]. Based on self-assembled monolayer (SAM) method, a protein layer can be fabricated by binding proteins to a substrate either covalently (chemical coupling) or non-covalently (physical absorption) [ 9 - 12 ], but the covalent method is superior due to its good reproducibility and homogeneity in layer formation [ 13 , 14 ].…”

Section: Introductionmentioning

confidence: 99%

Preparation and Characterization of Covalently Binding of Rat Anti-human IgG Monolayer on Thiol-Modified Gold Surface

Wang

Deng

et al. 2009

Nanoscale Res Lett

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The 16-mercaptohexadecanoic acid (MHA) film and rat anti-human IgG protein monolayer were fabricated on gold substrates using self-assembled monolayer (SAM) method. The surface properties of the bare gold substrate, the MHA film and the protein monolayer were characterized by contact angle measurements, atomic force microscopy (AFM), grazing incidence X-ray diffraction (GIXRD) method and X-ray photoelectron spectroscopy, respectively. The contact angles of the MHA film and the protein monolayer were 18° and 12°, respectively, all being hydrophilic. AFM images show dissimilar topographic nanostructures between different surfaces, and the thickness of the MHA film and the protein monolayer was estimated to be 1.51 and 5.53 nm, respectively. The GIXRD 2θ degrees of the MHA film and the protein monolayer ranged from 0° to 15°, significantly smaller than that of the bare gold surface, but the MHA film and the protein monolayer displayed very different profiles and distributions of their diffraction peaks. Moreover, the spectra of binding energy measured from these different surfaces could be well fitted with either Au4f, S2p or N1s, respectively. Taken together, these results indicate that MHA film and protein monolayer were successfully formed with homogeneous surfaces, and thus demonstrate that the SAM method is a reliable technique for fabricating protein monolayer.

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Section: Introductionmentioning

confidence: 99%

Preparation and Characterization of Covalently Binding of Rat Anti-human IgG Monolayer on Thiol-Modified Gold Surface

Wang

Deng

et al. 2009

Nanoscale Res Lett

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“…Previous studies have highlighted the importance of taking reaction environmental factors into account when designing ligand – receptor reactions, and have addressed factors such as steric hindrance to play a large role in the effectiveness of the interaction specificity. The use of homogeneous biotin-terminated Self-Assembled Monolayers are known to introduce steric hindrance between immobilized Streptavidin ligands during the binding process on the monolayer surface [21, 22]. The use of mixed Self-Assembled Monolayers, i,e.…”

Section: Introductionmentioning

confidence: 99%

Quantifying formations of Neutravidin clusters on biotinylated mixed silane Self-Assembled Monolayers

Ghosh

Neumann²

2022

Preprint

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Towards the goal of developing bio-chip/lab-on-a-chip substrates capable of performing highly specific bio-chemical reactions, Neutravidin binding to mixed Biotinylated Silane Self-Assembled Monolayers were studied using Confocal Fluorescence Light Microscopy. Non-specific bindings, specifically the formations of Neutravidin clusters, were quantified. Several experiments were conducted to determine the concentrations of Neutravidin necessary to not saturate surface binding to Biotinylated Self-Assembled Monolayers, determine the effectiveness of using FBS blocking buffers to reduce non-specific binding, optimize the repeatability of Neutravidin binding to Biotinlyated mixed Self-Assembled Monolayers with Silane-PEG-Biotin compositions ranging from 0 to 15%, and quantify background Neutravidin bindings and the corresponding formations of Neutravidin clusters to Self-Assembled Monolayers as Silane-PEG-Biotin percent compositions increase from 0 to 15%. The Neutravidin, Silane-PEG-Biotin, and Silane mPEG concentrations and ratios needed to develop homogeneous Neutravidin films, without the formations of clusters, on the Self-Assembled Monolayers have been determined.

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“…Protein molecules immobilized on a solid support holds special importance in antibody-antigen based biosensors, biomaterials and biophysical researches [1][2][3][4][5] . Protein molecules may be immobilized via physical adsorption, or electrostatic entrapment, etc.…”

Section: Introductionmentioning

confidence: 99%

Self-Assembled Human IgG Monolayers on Mixed Thiols Modified Gold Surfaces

Lv¹,

Wang²,

Chen³

2013

Asian J. Chem.

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The human IgG protein monolayers were fabricated on mixed thiols modified gold substrates by self-assembled monolayers method. The surface properties of protein monolayers were characterized by contact angle measurements, X-ray photoelectron spectroscopy and atomic force microscopy, respectively. It was found that the contact angles of the protein layers on the mixed thiols films containing 20 %, 40 %, 60 %, 80 %, 100 % of 16-mercaptohexadecanoic acid were 83.5 ± 3.3º, 56.7 ± 3.1º, 38.6 ± 2.9º, 25.8 ± 2.6º, 14.2 ± 2.3º, respectively. The atomic concentration of nitrogen of protein layers on pure 16-mercaptohexadecanoic acid film was counted to be 11.43 ± 0.56 %. Depth profile analysis showed the protein layer and 16-mercaptohexadecanoic acid film have the thickness of 7 nm and 2 nm, respectively. Furthermore, the adhesive forces between antibody and antigen layers with molar ratios of 16-mercaptohexadecanoic acid of 0, 0.2, 0.4, 0.6, 0.8 and 1.0 were determined to be 11 ± 2, 158 ± 21, 325 ± 24, 589 ± 36, 814 ± 41, 883 ± 45 pN, respectively. In summary, these results suggested that the human IgG protein monolayers were successfully formed and the surface coverage of protein molecules increased parallel with the increasing of 16-mercaptohexadecanoic acid content. Thus, they demonstrated that the mixed thiols based selfassembled monolayers method is a reliable technique for fabricating protein monolayers with adjustable surface coverage and good controllability.

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Analysis of a non-labeling protein array on biotin modified gold surfaces using atomic force microscopy and surface plasmon resonance

Cited by 16 publications

References 20 publications

Preparation and Characterization of Covalently Binding of Rat Anti-human IgG Monolayer on Thiol-Modified Gold Surface

Preparation and Characterization of Covalently Binding of Rat Anti-human IgG Monolayer on Thiol-Modified Gold Surface

Quantifying formations of Neutravidin clusters on biotinylated mixed silane Self-Assembled Monolayers

Self-Assembled Human IgG Monolayers on Mixed Thiols Modified Gold Surfaces

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