ArticleAnalytical chemistry2014
General approach for characterizing in vitro selected peptides with protein binding affinity.
Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Nanomaterial and interface advances in immunoassay biosensors.The journal of physical chemistry. C, Nanomaterials and interfaces · 2022Article
- Directing evolution of novel ligands by mRNA display.Chemical Society reviews · 2021Review
- Mechanistic and quantitative insight into cell surface targeted molecular imaging agent design.Scientific reports · 2016Article
- High-Throughput Measurement of Binding Kinetics by mRNA Display and Next-Generation Sequencing.Angewandte Chemie (International ed. in English) · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
In vitro selection technologies are important tools for identifying high affinity peptides to proteins of broad medical and biological interest. However, the technological advances that have made it possible to generate long lists of candidate peptides have far outpaced our ability to characterize the binding properties of individual peptides. Here, we describe a low cost strategy to rapidly synthesize, purify, screen, and characterize peptides for high binding affinity. Peptides are assayed in a 96-well dot blot apparatus using membranes that enable partitioning of bound and unbound peptide-protein complexes. We have validated the binding affinity constants produced by this method using known peptide ligands and applied this process to discover five new peptides with nanomolar affinity to human α-thrombin. Given the need for new analytical tools that can accelerate peptide discovery and characterization, we feel that this approach would be useful to a wide range of technologies that utilize high affinity peptides.
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Registered trials
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