Phage-displayed peptide libraries

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Screening phage-displayed combinatorial peptide libraries.

Among the many techniques available to investigators interested in mapping protein-protein interactions is phage display. With a modest amount of effort, time, and cost, one can select peptide ligands to a wide array of targets from phage-display combinatorial peptide libraries. In this article, protocols and examples are provided to guide scientists who wish to identify peptide ligands to thei...

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Identifying reactive peptides from phage-displayed libraries.

Phage display enables the synthesis, selection, and screening of large, polypeptide libraries (>1 × 10(10) different members). Selections from such libraries can identify binding partners to essentially any desired target (Sarikaya et al., Annu Rev Mater Res 34:373-408, 2004; Deutscher, Chem Rev 110:3196-3211, 2010). Peptides with affinity or reactivity to small molecule probes are attractive f...

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Mimotope identification using phage displayed random peptide libraries against monoclonal antibodies specific to house dust mite.

Random heptapeptide T7 and random 12mer M13 phage libraries were employed to identify mimotopes binding to monoclonal antibodies (MAb) specific to house dust mite. After selection of bound phage by bio-panning and determination of binding specificity, DNA of selected bound phages was amplified, sequenced and aligned for peptide similarity. Eight mimotopes which were partially matched with Der f...

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Identification of novel inhibitors of Pseudomonas aeruginosa MurC enzyme derived from phage-displayed peptide libraries.

OBJECTIVES The machinery of peptidoglycan biosynthesis is an ideal site at which to look for novel antimicrobial targets. Phage display was used to develop novel peptide inhibitors for MurC, an essential enzyme involved in the early steps of biosynthesis of peptidoglycan monomer. METHODS We cloned and overexpressed the murA, -B and -C genes from Pseudomonas aeruginosa in the pET expression ve...

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Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries.

We have used the Src homology 3 (SH3) domain to screen two phage-displayed random peptide libraries, each containing 2 x 10(8) unique members, and have identified a series of high affinity peptide ligands. The peptides possess similar proline-rich regions, which yield a consensus Src SH3-binding motif of RPLPPLP. We have confirmed this motif by screening a phage-displayed peptide library biased...

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ژورنال

عنوان ژورنال: Current Opinion in Biotechnology

سال: 1998

ISSN: 0958-1669

DOI: 10.1016/s0958-1669(98)80017-7