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Interaction Analysis through Proteomic Phage Display
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Ivarsson)
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Ivarsson)
2014 (English)In: BioMed Research International, ISSN 2314-6133, E-ISSN 2314-6141, 176172- p.Article, review/survey (Refereed) Published
Abstract [en]

Phage display is a powerful technique for profiling specificities of peptide binding domains. The method is suited for the identification of high-affinity ligands with inhibitor potential when using highly diverse combinatorial peptide phage libraries. Such experiments further provide consensus motifs for genome-wide scanning of ligands of potential biological relevance. A complementary but considerably less explored approach is to display expression products of genomic DNA, cDNA, open reading frames (ORFs), or oligonucleotide libraries designed to encode defined regions of a target proteome on phage particles. One of the main applications of such proteomic libraries has been the elucidation of antibody epitopes. This review is focused on the use of proteomic phage display to uncover protein-protein interactions of potential relevance for cellular function. The method is particularly suited for the discovery of interactions between peptide binding domains and their targets. We discuss the largely unexplored potential of this method in the discovery of domain-motif interactions of potential biological relevance.

Place, publisher, year, edition, pages
2014. 176172- p.
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:uu:diva-232438DOI: 10.1155/2014/176172ISI: 000346007900001OAI: oai:DiVA.org:uu-232438DiVA: diva2:748011
Funder
Swedish Research Council
Available from: 2014-09-18 Created: 2014-09-18 Last updated: 2017-12-05Bibliographically approved

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Interaction Analysis through Proteomic Phage Display(2492 kB)345 downloads
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Sundell, GustavIvarsson, Ylva

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