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Journal ArticleDOI

Searching for Peptide Ligands With an Epitope Library

Jamie K. Scott, +1 more
- 27 Jul 1990 - 
- Vol. 249, Iss: 4967, pp 386-390
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TLDR
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".
Abstract
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.

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Citations
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Journal ArticleDOI

Bacteriophage display and discovery of peptide leads for drug development

TL;DR: This review, though not comprehensive with respect to the explosive volume of phage display work over the last few years, focuses on recent developments in phage-displayed peptide technology.
Journal ArticleDOI

Mono‐ and Bivalent Antibody Fragments Produced in Escherichia coli: Engineering, Folding and Antigen Binding

TL;DR: The technology to produce monoclonal antibodies has led to the determination of an enormous number of antibody sequences, mostly from the cloned DNA sequence, crucial for defining consensus sequences, which allowed rapid cloning of antibody genes by the polymerase chain reaction (PCR), thereby generating even more sequence information.
Journal ArticleDOI

One-bead–one-structure combinatorial libraries

TL;DR: Direct methods of structure identification as well as indirect “coding” methods facilitating the synthesis and screening of nonpeptide libraries are discussed, and the ability to use combinatorial libraries to optimize initially discovered leads is illustrated with examples using peptide libraries.
Patent

Human growth hormone variants

TL;DR: In this article, human growth hormone variants are disclosed having enhanced affinity for the growth hormone receptor and conjugated to one or more chemical groups, such as poly(ethylene glycol), which is believed to prolong the in vivo half-life of the variants.
Journal ArticleDOI

Screening of a Library of Phage-displayed Peptides Identifies Human Bcl-2 as a Taxol-binding Protein

TL;DR: It is demonstrated that peptides displayed on the surface of bacteriophage particles can mimic the ligand-binding properties of disordered regions of proteins.
References
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Book

Molecular Cloning: A Laboratory Manual

TL;DR: Molecular Cloning has served as the foundation of technical expertise in labs worldwide for 30 years as mentioned in this paper and has been so popular, or so influential, that no other manual has been more widely used and influential.
Journal ArticleDOI

DNA sequencing with chain-terminating inhibitors

TL;DR: A new method for determining nucleotide sequences in DNA is described, which makes use of the 2',3'-dideoxy and arabinon nucleoside analogues of the normal deoxynucleoside triphosphates, which act as specific chain-terminating inhibitors of DNA polymerase.
Journal ArticleDOI

Rapid and efficient site-specific mutagenesis without phenotypic selection.

TL;DR: The high efficiency, approximately equal to 10-fold greater than that observed using current methods without enrichment procedures, is obtained by using a DNA template containing several uracil residues in place of thymine, which is applied to mutations introduced via both oligonucleotides and error-prone polymerization.
Book ChapterDOI

Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction.

TL;DR: A method whereby a nucleic acid sequence can be exponentially amplified in vitro is described in the chapter, and the possibility of utilizing a heat-stable DNA polymerase is explored so as to avoid the need for addition of new enzyme after each cycle of thermal denaturation.
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