Chemical strategies for generating protein biochips.

  title={Chemical strategies for generating protein biochips.},
  author={Pascal Jonkheijm and Dirk Weinrich and Hendrik V Schr{\"o}der and Christof M. Niemeyer and Herbert Waldmann},
  journal={Angewandte Chemie},
  volume={47 50},
Protein biochips are at the heart of many medical and bioanalytical applications. Increasing interest has been focused on surface activation and subsequent functionalization strategies for immobilizing these biomolecules. Different approaches using covalent and noncovalent chemistry are reviewed; particular emphasis is placed on the chemical specificity of protein attachment and on retention of protein function. Strategies for creating protein patterns (as opposed to protein arrays) are also… 
Applications of Protein Biochips in Biomedical and Biotechnological Research
This Minireview highlights selected developments in the application of protein biochips in proteomics and biomarker research and for drug development.
Protein-modified porous silicon films for biomedical applications
This chapter reports the experience of the groups on protein (hydrophobin) modified-PSi optical structures using porous silicon (PSi)-based devices together with different classes of proteins.
Multicomponent protein patterning of material surfaces
Representative approaches for creating multicomponent protein patterning are presented and their potential for tailoring microenvironments for cells on biomaterials surfaces is discussed.
Chemoselective protein and peptide immobilization on biosensor surfaces.
The protocols described in this chapter were designed for use in a Biacore instrument, but should also be applicable to other SPR instruments and, with slight adjustments, to many other types of bioanalytical applications that rely on protein-functionalized surfaces.
Protein engineering for directed immobilization.
In this review, the state of the art of the different protein immobilization strategies that are commonly used today with a special focus on biosensor applications are discussed.
Bioorthogonal chemistry for site-specific labeling and surface immobilization of proteins.
This Account summarizes recent developments and applications of site-specific protein labeling and surface immobilization of proteins, with a special focus on contributions to these fields.
Immobilization strategies for small molecule, peptide and protein microarrays
  • M. Köhn
  • Chemistry, Biology
    Journal of peptide science : an official publication of the European Peptide Society
  • 2009
Protein, peptide and small molecule microarrays are valuable tools in biological research. In the last decade, substantial progress has been achieved to make these powerful technologies more reliable
Facile Protein Immobilization Using Engineered Surface-Active Biofilm Proteins
This work functionalizes an interfacial protein, BslA, with peptides that spontaneously react with their cognate protein partners (SpyTag and SnoopTag) to create patterned surfaces of protein monolayers displaying reactive tags and demonstrates that these surfaces can be functionalized rapidly, spontaneously, and specifically with proteins of interest attached to SpyCatcher or SnoopCatcher.
Biosensor surface chemistry for oriented protein immobilization and biochip patterning
This licentiate thesis is focused on two methods for protein immobilization to biosensor surfaces for future applications in protein microarray formats. The common denominator is a surface chemistr
Biofunctionalization of Polymeric Thin Films and Surfaces
This chapter discusses the sophisticated and optimized surface chemistry that allows the introduction of biologically active species and ligands at surfaces and on structured specimens, and the implementation of the important function of reduced or suppressed nonspecific adsorption of proteins receives particular attention.


Nanoscale protein patterning by imprint lithography
This technique achieves high throughput reproducible nanoscale protein patterns with high selectivity and retained biofunctionality, as demonstrated by interactions between patterned antibodies and their antigen.
A versatile method for direct and covalent immobilization of DNA and proteins on biochips.
A method is presented for the immobilization of aryl diazonium modified biomolecules by direct electro-grafting onto the surface of a conducting material to create effective on-chip sensing layers.
Chemoselective attachment of biologically active proteins to surfaces by expressed protein ligation and its application for "protein chip" fabrication.
This new method was used to immobilize two fluorescent proteins and a functional SH3 domain using a protein microarrayer and is based in the chemoselective reaction between a protein C-terminal alpha-thioester and a modified surface containing N-Terminal Cys residues.
Protein patterning based on electrochemical activation of bioinactive surfaces with hydroquinone-caged biotin.
A protein attachment and patterning method based on a hydroquinone-caged biotin surface that generates bioactive biotin by mild electrochemical perturbation and allows site-selective generation of bioactiveBiotin for the immobilization of target protein by using prepatterned electrode arrays is reported.
Intein-mediated biotinylation of proteins and its application in a protein microarray.
The advantage of the avidin/biotin linkage over his-tag/Ni-NTA strategies for protein immobilization is highlighted by its ability to withstand a variety of chemical conditions, which makes this new protein array compatible with most biological assays.
Semi-wet peptide/protein array using supramolecular hydrogel
A novel semi-wet peptide/protein microarray using a supramolecular hydrogel composed of glycosylated amino acetate that overcomes several drawbacks of conventional protein chips, and thus can have potential applications in pharmaceutical research and diagnosis.
Photochemical surface patterning by the thiol-ene reaction.
The photochemical coupling of olefins to thiols to generate a stable thioether bond for the covalent surface patterning of proteins and small molecules is reported and indicates that thecovalent attachment of biotin to the surface occurs specifically through the proposed thiol-ene reaction and that the nonspecific adsorption ofBiotin is insignificant.
Self-aligned immobilization of proteins utilizing PEG patterns
A novel self-aligned method to selectively immobilize proteins on a silicon dioxide surface is developed in conjunction with a standard lift-off patterning technique of a PEG layer. The approach is
Immobilized hydrogels for screening of molecular interactions.
This work has designed, prepared, and evaluated immobilized hydrogels as general screening chambers for small molecule-protein, protein- protein, and nucleic acid-nucleic acid interactions and physically entraps the target complement within the polymer network and thus offers advantages over the conventional chips.