Site-selective protein immobilization by Staudinger ligation.

  title={Site-selective protein immobilization by Staudinger ligation.},
  author={Anja Watzke and Maja K{\"o}hn and Marta Guti{\'e}rrez-Rodr{\'i}guez and Ron Wacker and Hendrik V Schr{\"o}der and Rolf Breinbauer and Jürgen Kuhlmann and Kirill Alexandrov and Christof M. Niemeyer and Roger S. Goody and Herbert Waldmann},
  journal={Angewandte Chemie},
  volume={45 9},
A sticky situation: A site-specific immobilization of proteins onto a glass surface may allow the creation of protein microarrays. This approach relies on the Staudinger ligation between azide-modified proteins and a phosphane-functionalized glass surface. 
Oriented immobilization of farnesylated proteins by the thiol-ene reaction.
This method enables the oriented covalent immobilization of proteins directly from expression lysates without additional purification or derivatization steps.
General method for site-specific protein immobilization by Staudinger ligation.
This strategy provides a general means to fabricate microarrays displaying proteins in a uniform orientation by installing an azido group at the C-terminus of a model protein by using the method of expressed protein ligation and a synthetic bifunctional reagent.
Surface immobilization of biomolecules by click sulfonamide reaction.
Alkyne-modified biomolecules can be immobilized site- and chemoselectively on sulfonylazide slides under very mild conditions by means of the click sulfonamide reaction.
Oxo-ester mediated native chemical ligation on microarrays: an efficient and chemoselective coupling methodology.
This chemoselective method generates stable amide linkages without using any thiol additives and coupling of peptides and glycoconjugates bearing N-terminal cysteines to activated surfaces is reported.
A nucleoside triphosphate for site-specific labelling of DNA by the Staudinger ligation.
A novel nucleotide building block for enzymatic synthesis of azide modified DNA and subsequent conjugation via Staudinger ligation was developed.
Direct immobilization of oxyamine-modified proteins from cell lysates.
Oxyamine-modified proteins can be efficiently and selectively immobilized on ketone-coated glass slides at neutral pH in short reaction times by direct treatment and spotting of protein expression
Covalent Attachment of Proteins to Solid Supports and Surfaces via Sortase-Mediated Ligation
The Sortase A transpeptidase of S. aureus provides a general, robust, and gentle approach to the selective covalent immobilization of proteins on three very different solid supports.
Oriented protein immobilization using covalent and noncovalent chemistry on a thiol-reactive self-reporting surface.
The fabrication of a patterned protein array is reported using three orthogonal methods of immobilization that are detected exploiting a fluorogenic surface providing a means to visualize the immobilization even of nonfluorescent biomolecules.
Site‐Specific Protein and Peptide Immobilization on a Biosensor Surface by Pulsed Native Chemical Ligation
This communication describes the facile and direct site-specific immobilization of proteins and peptides on a biosensor surface by using the native chemical ligation (NCL) reaction, which allows control of both the orientation of the ligand presented at the surface, as well as its density in a highly programmable manner.


Site-specific protein immobilization by Staudinger ligation.
The Staudinger ligation between an azido-protein and a phosphinothioester-derivatized surface is demonstrated to be an effective means for the site-specific, covalent immobilization of a protein.
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.
The Staudinger ligation-a gift to chemical biology.
The current state of knowledge on the Staudinger ligation and its application both for the preparation of bioconjugates and as a ligation method in chemical biology are described.
Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
It is shown that proteins containing azidohomoalanine can be selectively modified in the presence of other cellular proteins by means of Staudinger ligation with triarylphosphine reagents and incorporation of azide-functionalized amino acids into proteins in vivo provides opportunities for protein modification under native conditions and selective labeling of proteins in the intracellular environment.
Dendrimer‐Activated Solid Supports for Nucleic Acid and Protein Microarrays
The results indicate that the novel dendrimer‐activated surfaces display a surface coverage with capture oligomers about twofold greater than that with conventional microarrays containing linear chemical linkers.
Intein-Mediated Synthesis of Proteins Containing Carbohydrates and Other Molecular Probes
We report here the use of an intein-mediated protein ligation strategy for the synthesis of glycoproteins and proteins containing various molecular probes. Several simple cysteine derivatives are
Probing glycosyltransferase activities with the Staudinger ligation.
A novel glycosyltransferase assay that exploits their unnatural substrate tolerance and the unique chemical reactivity of the azide is described, applicable to any glycosoltransferase or group-transfer enzyme that tolerates unnatural azido substrates.
Printing proteins as microarrays for high-throughput function determination.
Miniaturized assays that accommodate extremely low sample volumes and enable the rapid, simultaneous processing of thousands of proteins are developed to facilitate subsequent studies of protein function.