ArticleBioconjugate chemistry2008
High-throughput method for ranking the affinity of peptide ligands selected from phage display libraries.
Article in Bioconjugate chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Capsid-engineered AAV vector overcomes a key intracellular barrier and efficiently transduces spiral ganglion neurons in adult mice.Molecular therapy. Advances · 2026Article
- Evolving a Peptide: Library Platforms and Diversification Strategies.International journal of molecular sciences · 2019Review
- Fluorescent "Turn off-on" Small-Molecule-Monitoring Nanoplatform Based on Dendrimer-like Peptides as Competitors.ACS applied materials & interfaces · 2019Article
- PuLSE: Quality control and quantification of peptide sequences explored by phage display libraries.PloS one · 2018Article
- Continuous microfluidic assortment of interactive ligands (CMAIL).Scientific reports · 2016Article
- Competitive and noncompetitive phage immunoassays for the determination of benzothiostrobin.Analytica chimica acta · 2015Article
- Drop-out phagemid vector for switching from phage displayed affinity reagents to expression formats.Analytical biochemistry · 2011Article
- Phage-displayed combinatorial peptide libraries in fusion to beta-lactamase as reporter for an accelerated clone screening: Potential uses of selected enzyme-linked affinity reagents in downstream applications.Combinatorial chemistry & high throughput screening · 2010Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The use of phage display peptide libraries allows rapid isolation of peptide ligands for any target selector molecule. However, due to differences in peptide expression and the heterogeneity of the phage preparations, there is no easy way to compare the binding properties of the selected clones, which operates as a major "bottleneck" of the technology. Here, we present the development of a new type of library that allows rapid comparison of the relative affinity of the selected peptides in a high-throughput screening format. As a model system, a phage display peptide library constructed on a phagemid vector that contains the bacterial alkaline phosphatase gene (BAP) was selected with an antiherbicide antibody. Due to the intrinsic switching capacity of the library, the selected peptides were transferred "en masse" from the phage coat protein to BAP. This was coupled to an optimized affinity ELISA where normalized amounts of the peptide-BAP fusion allow direct comparison of the binding properties of hundreds of peptide ligands. The system was validated by plasmon surface resonance experiments using synthetic peptides, showing that the method discriminates among the affinities of the peptides within 3 orders of magnitude. In addition, the peptide-BAP protein can find direct application as a tracer reagent.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.