Artificial Polypeptide Scaffold for Protein Immobilization

Zhang, Kechun; Diehl, Michael R.; Tirrell, David A.

doi:10.1021/ja051457h

Cited by 147 publications

(135 citation statements)

References 22 publications

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“…This procedure is more popular for the immobilization of Abs as compared to enzymes. Besides avidin−biotin, recombinant proteins can be selectively attached to an artificial polypeptide scaffold system via heterodimeric association of a separate leucine zipper pair consisting of 43 amino acids with an affinity constant of 10 −15 M. 161 The capture ligand approach involving the use of protein transsplicing mechanism deserves a brief comment here because this approach can offer some potential in biomolecule immobilization. Intein fragments exhibits protein splicing activity, and the intein self-processing domain can split into two fragments: the former is incorporated to the target biomolecule, whereas the latter is attached to the APTES-modified surface.…”

Section: Affinitymentioning

confidence: 99%

Immobilization of Antibodies and Enzymes on 3-Aminopropyltriethoxysilane-Functionalized Bioanalytical Platforms for Biosensors and Diagnostics

et al. 2014

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/npsi/ctrl?lang=en http://nparc.cisti-icist.nrc-cnrc.gc.ca/npsi/ctrl?lang=fr READ THESE TERMS AND CONDITIONS CAREFULLY BEFORE USING THIS WEBSITE.http://nparc.cisti-icist.nrc-cnrc.gc.ca/npsi/jsp/nparc_cp.jsp?lang=en Vous avez des questions? Nous pouvons vous aider. Pour communiquer directement avec un auteur, consultez la première page de la revue dans laquelle son article a été publié afin de trouver ses coordonnées. Si vous n'arrivez pas à les repérer, communiquez avec nous à PublicationsArchive-ArchivesPublications@nrc-cnrc.gc.ca.

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Section: Affinitymentioning

confidence: 99%

Immobilization of Antibodies and Enzymes on 3-Aminopropyltriethoxysilane-Functionalized Bioanalytical Platforms for Biosensors and Diagnostics

et al. 2014

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“…For example, a fusion protein of ELP with protein A, G, or L can bind to an antibody and act as a concentration mechanism to enhance signals [334] (Figure 23). A similar strategy can be used to immobilize recombinant proteins through the interaction between the leucine zipper pairs [335]. In addition, this makes it possible to individually address biomolecules on surfaces by immobilizing the biomolecules in a spatial controlled manner using local environmental changes [336].…”

Section: Biosensing-detectionmentioning

confidence: 99%

Peptide-based biopolymers in biomedicine and biotechnology

Chow

Nunalee

Lim

et al. 2008

Materials Science and Engineering: R: Reports

286

231

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Peptides are emerging as a new class of biomaterials due to their unique chemical, physical, and biological properties. The development of peptide-based biomaterials is driven by the convergence of protein engineering and macromolecular self-assembly. This review covers the basic principles, applications, and prospects of peptide-based biomaterials. We focus on both chemically synthesized and genetically encoded peptides, including poly-amino acids, elastin-like polypeptides, silk-like polymers and other biopolymers based on repetitive peptide motifs. Applications of these engineered biomolecules in protein purification, controlled drug delivery, tissue engineering, and biosurface engineering are discussed.

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“…For example, Zhang et al incorporated two artificial leucine zipper domains into their protein chips as a means of protein immobilization (60). In this work, one of two matching zippers was fixed to a glass slide and then used to trap recombinant proteins fused to the complementary zipper.…”

Section: Discussionmentioning

confidence: 99%

Protein Interaction Module–assisted Function X (PIMAX) Approach to Producing Challenging Proteins Including Hyperphosphorylated Tau and Active CDK5/p25 Kinase Complex

Sui

et al. 2015

Molecular & Cellular Proteomics

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Many biomedically critical proteins are underrepresented in proteomics and biochemical studies because of the difficulty of their production in Escherichia coli. These proteins might possess posttranslational modifications vital to their functions, tend to misfold and be partitioned into bacterial inclusion bodies, or act only in a stoichiometric dimeric complex. Successful production of these proteins requires efficient interaction between these proteins and a specific "facilitator," such as a protein-modifying enzyme, a molecular chaperone, or a natural physical partner within the dimeric complex. Here we report the design and application of a protein interaction moduleassisted function X (PIMAX) system that effectively overcomes these hurdles. By fusing two proteins of interest to a pair of well-studied protein-protein interaction modules, we were able to potentiate the association of these two proteins, resulting in successful production of an enzymatically active cyclin-dependent kinase complex and hyperphosphorylated tau protein, which is intimately linked to Alzheimer disease. Furthermore, using tau isoforms quantitatively phosphorylated by GSK-3␤ and CDK5 kinases via PIMAX, we demonstrated the hyperphosphorylation-stimulated tau oligomerization in vitro, paving the way for new Alzheimer disease drug discoveries. Vectors for PIMAX can be easily modified to meet the needs of different applications. This approach thus provides a convenient and modular suite with broad implications for proteomics and biomedical research. Molecular & Cellular Proteomics

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Artificial Polypeptide Scaffold for Protein Immobilization

Cited by 147 publications

References 22 publications

Immobilization of Antibodies and Enzymes on 3-Aminopropyltriethoxysilane-Functionalized Bioanalytical Platforms for Biosensors and Diagnostics

Immobilization of Antibodies and Enzymes on 3-Aminopropyltriethoxysilane-Functionalized Bioanalytical Platforms for Biosensors and Diagnostics

Peptide-based biopolymers in biomedicine and biotechnology

Protein Interaction Module–assisted Function X (PIMAX) Approach to Producing Challenging Proteins Including Hyperphosphorylated Tau and Active CDK5/p25 Kinase Complex

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