Filamentous Phage Display in the New Millennium

Kehoe, John W.; Kay, Brian K.

doi:10.1021/cr000261r

Cited by 359 publications

(269 citation statements)

References 339 publications

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“…It has been applied to identify binding peptides for a wide range of molecules, such as proteins, nucleic acids, and small molecules. [11][12][13] This study and those of several other groups have shown its utility for selecting peptides that recognize and bind to solid surfaces and particles. [14][15][16] Some of these peptides have been incorporated into new biomaterials that offer novel interfacial binding functionalities.…”

Section: Discussionmentioning

confidence: 89%

A recombinant triblock protein polymer with dispersant and binding properties for digital printing

Qin

O’Brien

2008

Biopolymers

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A structured triblock protein was designed to explore the potential of engineered peptides to function as high‐performance ink dispersants and binders. The protein consists of three functional elements, including a pigment binding domain, a hydrophilic linker, and a printing surface binding domain. To construct such a chimeric protein, a carbon black binding peptide, FHENWPS, and a cellulose binding peptide, THKTSTQRLLAA, were identified from phage display libraries through biopanning, based on their strong and specific binding affinities to carbon black and cellulose. They were used as carbon black and cellulose binding domains, respectively, in a recombinant triblock protein. A linker sequence, PTPTPTPTPTPTPTPTPTPTPTP, was adapted from endoglucanase A of the bacterium Cellulomonas fimi, as a small, rigid, and hydrophilic interdomain linker. When incorporated into the triblock structure between the carbon black and cellulose binding sequences, the linker sufficiently isolates these two elements and allows dual binding activity. The structured triblock protein was shown to disperse carbon black particles and attach it to paper surfaces. Thus, the utility of structured proteins having useful dispersant and binding properties for digital printing inks was demonstrated. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90: 28–36, 2008. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Section: Discussionmentioning

confidence: 89%

A recombinant triblock protein polymer with dispersant and binding properties for digital printing

Qin

O’Brien

2008

Biopolymers

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“…[48] Die "Landscape"-Phagen-Bibliothek wurde von Petrenko, Smith und Mitarbeitern entwickelt. [51,53] [35,54,55] und Büchern beschrieben. [36][37][38] Sie war bei der Entwicklung von Impfstoffen und Antikörpern erfolgreich und hat sich bei der Untersuchung von Protein-ProteinWechselwirkungen sowie beim Protein-Engineering bewährt.…”

Section: Das Phagendisplay Als Technik Zur Identifizierung Von Zielspunclassified

Die Anwendung von Viren in Chemo‐ und Biosensoren

2009

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Viren haben sich in jüngster Zeit als einzigartige Hilfsmittel für den empfindlichen und selektiven Nachweis von Analyten wie Explosivstoffen, Proteinen, Bakterien, Viren, Sporen und Toxinen erwiesen. Auf Bakterien spezialisierte Viren, die Bakteriophagen – oder kurz Phagen –, wurden dabei am intensivsten untersucht: Zielspezifische nichtlysierende Phagen (sowie von diesen präsentierte Peptide und Proteine) können mithilfe hoch entwickelter Phagendisplaytechniken identifiziert werden, und lysierende Phagen können gezielt Bakterien aufbrechen und spezifische Zellmarker wie Enzyme ausschütten, die analysiert werden können. Darüber hinaus sind Phagen chemisch wie thermisch hinreichend stabil, und sie lassen sich mit Molekülen kuppeln und mit Nanomaterialien kombinieren und auf der Oberfläche eines Signalwandlers in einem Analysesystems verankern. Im Mittelpunkt dieses Aufsatzes stehen Fortschritte bei der Verwendung von Phagen in Chemo‐ und Biosensoren durch Kombination mit etablierten analytischen Techniken. Überdies werden aktuelle Entwicklungen bei der Verwendung von Virus‐Nanomaterial‐Kompositen und anderen Viren in Sensoranwendungen vorgestellt.

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“…28,29 Other chemical modifications have been used to create specific biological interactions. 30 To gain a greater degree of architectural control, it would be valuable to have a detailed understanding of the principles by which the viral particles are constructed. The tobacco mosaic virus can be assembled in vitro by mixing its single-stranded RNA with the 17.5 kDa capsid protein under the proper conditions.…”

Section: Introductionmentioning

confidence: 99%

Programmed assembly of nanoscale structures using peptoids.

Ren

Russell

Morishetti

et al. 2011

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Sequence-specific polymers are the basis of the most promising approaches to bottom-up programmed assembly of nanoscale materials. Examples include artificial peptides and nucleic acids. Another class is oligo(N-functional glycine)s, also known as peptoids, which permit greater sidegroup diversity and conformational control, and can be easier to synthesize and purify. We have developed a set of peptoids that can be used to make inorganic nanoparticles more compatible with biological sequencespecific polymers so that they can be incorporated into nucleic acid or other biologically based nanostructures. Peptoids offer degrees of modularity, versatility, and predictability that equal or exceed other sequence-specific polymers, allowing for rational design of oligomers for a specific purpose. This degree of control will be essential to the development of arbitrarily designed nanoscale structures. 5 ACKNOWLEDGMENTS

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Filamentous Phage Display in the New Millennium

Cited by 359 publications

References 339 publications

A recombinant triblock protein polymer with dispersant and binding properties for digital printing

A recombinant triblock protein polymer with dispersant and binding properties for digital printing

Die Anwendung von Viren in Chemo‐ und Biosensoren

Programmed assembly of nanoscale structures using peptoids.

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