Nanometric Protein Arrays on Protein-Resistant Monolayers on Silicon Surfaces

Gu, Jianhua; Yam, Chi Ming; Li, Sha; Cai, Chengzhi

doi:10.1021/ja048405x

Cited by 123 publications

(144 citation statements)

References 18 publications

Supporting

Mentioning

141

Contrasting

Order By: Relevance

“…SPL methods enable researchers to selectively and intentionally change the surface chemistry of small areas under the tip of an atomic force or scanning tunneling microscope. Bias-induced nanolithography, dip-pen nanolithography (DPN), catalyticprobe lithography, and nanografting are types of SPL with different writing mechanisms (20)(21)(22)(23)(24)(25). The height and surface chemistry of nanopatterns can be tailored by the selection of molecules to be patterned, with designated chain lengths and surface groups.…”

Section: Afm-based Lithography With Samsmentioning

confidence: 99%

AFM-Based Lithography for Nanoscale Protein Assays

Ngunjiri

Garno²

2008

Anal. Chem.

View full text Add to dashboard Cite

I magine the tremendous revolution in medical diagnostics if we had the ability to screen thousands of proteins in an immunosensing array by using a single drop of serum and a biochip the size of the head of a pin! Scientists have begun to explore the frontier of nanoscale chemistry to attain the ultimate miniaturization for protein assays by using atomic force microscopy (AFM). Of course, we have a long way to go before we achieve such futur-istic technology. At this point, researchers have begun to develop analytical methods for detecting proteins by using nanoscale surface assays. This article describes recent efforts to develop nanoscale protein assays with AFM-based lithography.There are many practical reasons for developing protein assays at the nanoscale. New information can be gained to address fundamental questions about protein binding and AFM-BAsed LithogrAphy For NANoscALe proteiN AssAys scanning probe lithography offers new possibilities for nanoscale investigations of protein binding.

show abstract

Section: Afm-based Lithography With Samsmentioning

confidence: 99%

AFM-Based Lithography for Nanoscale Protein Assays

Ngunjiri

Garno²

2008

Anal. Chem.

View full text Add to dashboard Cite

show abstract

“…27,33 Bovine serum albumin (BSA) has been patterned using SNP, 11 DPN, 24 and conductive AFM (c-AFM ). 37 Another important protein, avidin/streptavidin has been patterned with various techniques: DPN, 24,38 c-AFM. 37 Protein G has been patterned with E-NFP 9 and NFP.…”

Section: Proteinsmentioning

confidence: 99%

“…37 Another important protein, avidin/streptavidin has been patterned with various techniques: DPN, 24,38 c-AFM. 37 Protein G has been patterned with E-NFP 9 and NFP. 10 Other 12 µm examples of proteins include his-tagged peptides with E-DPN, 28 his-tagged ubiquitin and thioredoxin with DPN 36 and GFP printed with NFP.…”

Section: Proteinsmentioning

confidence: 99%

Nanobiolithography of Biochips

Gheber

2007

Handbook of Biosensors and Biochips

View full text Add to dashboard Cite

The maturation of arrayed biosensors (mainly DNA microarrays, known as DNA chips ) has demonstrated the power of the parallel approach to sensing in general and biosensing in particular. The ability to ask thousands of questions and obtain simultaneous answers enables high‐throughput screening of potential drugs, diagnosis of genetically derived disorders, and basic genome research. The promise of the biochip, though, goes much further and farther: online monitoring of drinking water and food quality, point‐of‐care diagnosis, biodefense, and other futuristic applications. To reach there, though, there is a need to almost completely transform the existing technology, which at present is highly localized to large research laboratories, big pharmaceutical companies, or advanced medical centers. Several aspects must be considered simultaneously (a step‐by‐step improvement of existing technology is likely to fail): the “spot” size needs to be reduced by several orders of magnitude, reporting and reading systems must be integrated, sample preparation and handling subsystems should also be integrated, the devices need to be increasingly autonomous and have communication abilities, and label‐free detection methods need to be developed to enable on‐line operation. One possible avenue, nanobiolithography, has gained much attention during the past years. We review the problems and possible ways to solve them, using state‐of‐the‐art nanobiolithography techniques.

show abstract

“…Thus, the PEG-lipid addressed the problem of protein aggregation; however, the rebinding of ferritin was not evaluated. This approach to creating protein binding sites in monolayers is in contrast to work by Cai's group, which uses a similar principle of an inert oligoethyleneglycol molecule to shape the pockets in which protein is bound [43]. However, in that case nanolithography is used to form the binding pockets within the fixed monolayer instead of the self-assembly mechanism employed here.…”

Section: Introductionmentioning

confidence: 99%

Formation of protein molecular imprints within Langmuir monolayers: A quartz crystal microbalance study

Turner

Wright

Hlady

et al. 2007

Journal of Colloid and Interface Science

View full text Add to dashboard Cite

Protein imprinting leading to enhanced rebinding of ferritin to ternary lipid monolayers is demonstrated using a quartz crystal microbalance. Monolayers consisting of cationic dioctadecyldimethylammonium bromide, non-ionic methyl stearate, and poly(ethylene glycol) bearing phospholipids were imprinted with ferritin at the air/water interface of a Langmuir-Blodgett trough and transferred hydrated to hydrophobic substrates for study. This immobilization was shown by fluorescence correlation spectroscopy to significantly hinder any further diffusion of lipids, while rebinding studies demonstrated up to a six-fold increase in ferritin adsorption to imprinted versus control monolayers. A diminished rebinding of ferritin to its imprint was observed through pH reduction to below the protein isoelectric point, demonstrating the electrostatic nature of the interaction. Rebinding to films where imprint pockets remained occupied by the template protein was also minimal. Studies with a smaller acidic protein revealed the importance of the steric influence of poly(ethylene glycol) in forming the protein binding pockets, as albumin-imprinted monolayers showed low binding of ferritin, while ferritin-imprinted monolayers readily accommodated albumin. The controllable structure-function relationship and limitations of this system are discussed with respect to the application of protein imprinting in sensor development as well as fundamental studies of proteins at dynamic interfaces.

show abstract

Nanometric Protein Arrays on Protein-Resistant Monolayers on Silicon Surfaces

Cited by 123 publications

References 18 publications

AFM-Based Lithography for Nanoscale Protein Assays

AFM-Based Lithography for Nanoscale Protein Assays

Nanobiolithography of Biochips

Formation of protein molecular imprints within Langmuir monolayers: A quartz crystal microbalance study

Contact Info

Product

Resources

About