A new type of synthetic peptide library for identifying ligand-binding activity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-11

AUTHORS

K S Lam, S E Salmon, E M Hersh, V J Hruby, W M Kazmierski, R J Knapp

ABSTRACT

Our aim was to improve techniques for drug development by facilitating the identification of small molecules that bind with high affinity to acceptor molecules (for example, cell-surface receptors, enzymes, antibodies) and so to mimic or block their interaction with the natural ligand. Previously such small molecules have been characterized individually on a serial basis. The systematic synthesis and screening of peptide libraries of defined structure represents a new approach. For relatively small libraries, predetermined sequence variations on solid-phase supports have been used, and large libraries have been produced using a bacteriophage vector into which random oligodeoxynucleotide sequences have been introduced, but these techniques have severe limitations. Here we investigate an alternative approach to synthesis and screening of peptide libraries. Our simple methodology greatly enhances the production and rapid evaluation of random libraries of millions of peptides so that acceptor-binding ligands of high affinity can be rapidly identified and sequenced, on the basis of a 'one-bead, one-peptide' approach. More... »

PAGES

82-84

Journal

TITLE

Nature

ISSUE

6348

VOLUME

354

Author Affiliations

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  • Identifiers

    URI

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    DOI

    http://dx.doi.org/10.1038/354082a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1045350492

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1944576


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    18 schema:description Our aim was to improve techniques for drug development by facilitating the identification of small molecules that bind with high affinity to acceptor molecules (for example, cell-surface receptors, enzymes, antibodies) and so to mimic or block their interaction with the natural ligand. Previously such small molecules have been characterized individually on a serial basis. The systematic synthesis and screening of peptide libraries of defined structure represents a new approach. For relatively small libraries, predetermined sequence variations on solid-phase supports have been used, and large libraries have been produced using a bacteriophage vector into which random oligodeoxynucleotide sequences have been introduced, but these techniques have severe limitations. Here we investigate an alternative approach to synthesis and screening of peptide libraries. Our simple methodology greatly enhances the production and rapid evaluation of random libraries of millions of peptides so that acceptor-binding ligands of high affinity can be rapidly identified and sequenced, on the basis of a 'one-bead, one-peptide' approach.
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