Isolation of peptides from phage-displayed random peptide libraries that interact with the talin-binding domain of vinculin

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Isolation of peptides from phage-displayed random peptide libraries that interact with the talin-binding domain of vinculin.

Peptides isolated from combinatorial libraries typically interact with, and thus help to characterize, biologically relevant binding domains of target proteins. To characterize the binding domains of the focal adhesion protein vinculin, vinculin-binding peptides were isolated from two phage-displayed random peptide libraries. Altogether, five non-similar vinculin-binding peptides were identifie...

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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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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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Identification of high-affinity VEGFR3-binding peptides through a phage-displayed random peptide library

OBJECTIVE Vascular endothelial growth factor (VEGF) interaction with its receptor, VEGFR-3/Flt-4, regulates lymphangiogenesis. VEGFR-3/Flt-4 expression in cancer cells has been correlated with clinical stage, lymph node metastasis, and lymphatic invasion. The objective of this study is to identify a VEGFR-3/Flt-4-interacting peptide that could be used to inhibit VEGFR-3 for ovarian cancer thera...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1997

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3240523