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Highly selective cyclic peptide ligands for NeutrAvidin and avidin identified by phage display.

Highly selective cyclic peptide ligands for NeutrAvidin and avidin identified by phage display. Research Abstract Details 

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  • Highly selective cyclic peptide ligands for NeutrAvidin and avidin identified by phage display. Abstract Text:

    scott c meyerScott C Meyer,thomas gajThomas Gaj,indraneel ghoshIndraneel Ghosh,

    Screening combinatorial libraries of conformationally constrained peptides against macromolecular targets is utilized in identifying novel drug leads and in developing new reagents for chemical biology. In methods such as phage-display selections, biotinylated macromolecular targets are often immobilized on avidin- and streptavidin-functionalized supports. Thus, the characterization of peptides that bind avidin and streptavidin is necessary for accurate interpretation of screening and selection results. Toward this goal, we panned a phage-displayed cyclic peptide library against NeutrAvidin, a chemically deglycosylated version of avidin. The selection produced a highly homologous consensus motif (Asp-Arg/Leu-Ala-Ser/Thr-Pro-Tyr/Trp). Two of these cyclic peptides, CDRATPYC and CDRASPYC, bound both NeutrAvidin and avidin with low-micromolar dissociation constants, whereas their acyclic counterparts had negligible affinity (< 80-fold). Moreover, these cyclic peptides were very specific for their targets and did not bind the structurally and functionally similar protein, streptavidin. Thus, we have identified a new class of cyclic peptides, distinct from the much-studied streptavidin-binding His-Pro-Gln peptide motif. These results will not only allow for discriminating between desired and background cyclic peptide motifs in selections and screens but also provide a new protein/peptide model system and a useful reagent in chemical biology that can have utility in protein immobilization, purification, and chemical tagging.

    Highly selective cyclic peptide ligands for NeutrAvidin and avidin identified by phage display. Publishing Authors By Initials

    sc meyerSC Meyer,t gajT Gaj,i ghoshI Ghosh,

    For similar abstracts research abstracts see: abstracts research

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    Highly selective cyclic peptide ligands for NeutrAvidin and avidin identified by phage display. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Chemical biology & drug design

    VOLUME: 68

    Page Numbers: 3-10

    Journal Abbreviation:

    ISSN: 1747-0277

    DAY: 3

    MONTH: Jul

    YEAR: 2006

    Highly selective cyclic peptide ligands for NeutrAvidin and avidin identified by phage display. Information

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    LANGUAGE: eng

    NlmUniqueID: 101262549

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    Grant and Affiliation Information for Highly selective cyclic peptide ligands for NeutrAvidin and avidin identified by phage display.

    AFFILIATION: Department of Chemistry, University of Arizona, Tucson, AZ 85721, USA.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: Chem Biol Drug Des

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