Publication Date:
1990-07-27
Description:
Tens of millions of short peptides can be easily surveyed for tight binding to an antibody, receptor or other binding protein using an "epitope library." The library is a vast mixture of filamentous phage clones, each displaying one peptide sequence on the virion surface. The survey is accomplished by using the binding protein to affinity-purify phage that display tight-binding peptides and propagating the purified phage in Escherichia coli. The amino acid sequences of the peptides displayed on the phage are then determined by sequencing the corresponding coding region in the viral DNA's. Potential applications of the epitope library include investigation of the specificity of antibodies and discovery of mimetic drug candidates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, J K -- Smith, G P -- GM41478/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 27;249(4967):386-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Sciences, University of Missouri, Columbia 65211.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1696028" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Antibodies/immunology
;
Antibodies, Monoclonal/immunology
;
Bacteriophages/genetics/immunology/isolation & purification
;
Base Sequence
;
Cloning, Molecular
;
Epitopes/*genetics
;
Escherichia coli/genetics
;
*Gene Library
;
Genetic Vectors
;
Hemerythrin/analogs & derivatives/immunology
;
Ligands
;
Molecular Sequence Data
;
Peptides/*immunology
;
Transfection
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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