In vitro display technologies: novel developments and applications

Amstutz, Patrick; Forrer, Patrik; Zahnd, Christian; Plückthun, Andreas

doi:10.1016/s0958-1669(00)00234-2

Cited by 158 publications

(96 citation statements)

References 51 publications

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“…In the competitive KDR/VEGF blocking assay, various amounts of anti-KDR antibodies were mixed with a fixed amount of KDR-AP (100 ng) and incubated at room temperature for 1 h. The mixture were then transferred to 96-well microtiter plates precoated with VEGF165 (200 ng/ well) and incubated at room temperature for an additional 2 h, after which the plates were washed five times, and the substrate for AP was added, followed by reading the absorbance at 405 nm to quantify the bound KDR-AP molecules (10). IC 50 , i.e. the antibody concentration required for 50% inhibition of KDR binding to VEGF, was then calculated.…”

Section: Methodsmentioning

confidence: 99%

Tailoring in Vitro Selection for a Picomolar Affinity Human Antibody Directed against Vascular Endothelial Growth Factor Receptor 2 for Enhanced Neutralizing Activity

Lü¹,

Shen²,

Vil³

et al. 2003

Journal of Biological Chemistry

175

127

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Section: Methodsmentioning

confidence: 99%

Tailoring in Vitro Selection for a Picomolar Affinity Human Antibody Directed against Vascular Endothelial Growth Factor Receptor 2 for Enhanced Neutralizing Activity

Lü¹,

Shen²,

Vil³

et al. 2003

Journal of Biological Chemistry

175

127

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“…One way to achieve this is to use antibody engineering techniques, which associate in vitro-generated genetic diversity with selection procedures such as phage, ribosome or RNA display [107] to generate and screen for antibodies that are functional under highly denaturing conditions [108,109]. In this context, the heavychain camelid antibody fragments appear to be of particular interest.…”

Section: Conclusion and Future Prospectsmentioning

confidence: 99%

Probing the origins, diagnosis and treatment of amyloid diseases using antibodies

Dumoulin

Dobson

2004

Biochimie

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The deposition of proteins in the form of amyloid fibrils is the characteristic feature of more than 20 medical conditions affecting the central nervous system or a variety of peripheral tissues. These disorders, which include Alzheimer's disease, the prion diseases and type II diabetes, are of enormous importance in the context of present-day human health and welfare. Extensive research is therefore being carried out to define the molecular details of the mechanism of the pathological conversion of amyloidogenic proteins from their soluble forms into fibrillar structures. This review focuses on recent studies that demonstrate the power of using antibodies or antibody fragments to probe the process of fibril formation, and discusses the emerging potential of these species as diagnostic and therapeutic agents.

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“…Applications range from the examination of receptor-antibody interactions and the study of protein-ligand interactions to the isolation and directed evolution of enzymes and proteins for enhanced catalysis or altered binding characteristics. [61][62][63][64][65] Among the display technologies, the in vivo selection of peptides using cellsurface display (CSD) and phage display (PD) has been used most frequently (Figure 2). 9 CSD is a technology whereby peptides appear on the flagella of a bacterial cell membrane.…”

Section: Selection Of Inorganic-binding Peptides Using Combinatorial mentioning

confidence: 99%

“…Inorganic materials are very different substrates than proteinaceous or general biomolecular ligands. [61][62][63][64][65] Therefore, adapting biological display technologies for the realm of materials science would require a new set of conditions and protocols, though this has not been widely discussed in the literature so far. 55 Inorganic compounds come in a variety of forms, from morphologically uncharacterized powders of various particle sizes to single crystals with crystallographically defined flat surfaces.…”

Section: Selection Of Inorganic-binding Peptides Using Combinatorial mentioning

confidence: 99%

Molecular Biomimetics: Genetic Synthesis, Assembly, and Formation of Materials Using Peptides

Tamerler¹,

Sarıkaya²

2008

MRS Bull.

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In nature, the molecular-recognition ability of peptides and, consequently, their functions are evolved through successive cycles of mutation and selection. Using biology as a guide, it is now possible to select, tailor, and control peptide-solid interactions and exploit them in novel ways. Combinatorial mutagenesis provides a protocol to genetically select short peptides with specific affinity to the surfaces of a variety of materials including metals, ceramics, and semiconductors. In the articles of this issue, we describe molecular characterization of inorganic-binding peptides; explain their further tailoring using post-selection genetic engineering and bioinformatics; and finally demonstrate their utility as molecular synthesizers, erectors, and assemblers. The peptides become fundamental building blocks of functional materials, each uniquely designed for an application in areas ranging from practical engineering to medicine.

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In vitro display technologies: novel developments and applications

Cited by 158 publications

References 51 publications

Tailoring in Vitro Selection for a Picomolar Affinity Human Antibody Directed against Vascular Endothelial Growth Factor Receptor 2 for Enhanced Neutralizing Activity

Tailoring in Vitro Selection for a Picomolar Affinity Human Antibody Directed against Vascular Endothelial Growth Factor Receptor 2 for Enhanced Neutralizing Activity

Probing the origins, diagnosis and treatment of amyloid diseases using antibodies

Molecular Biomimetics: Genetic Synthesis, Assembly, and Formation of Materials Using Peptides

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