Identification of binding peptides of the ADAM15 disintegrin domain using phage display

Wu, Jang‐Yen; Wu, Minchen; Zhang, Lian-Fen; Lei, Jianyong; Feng, Lei; Jin, Jian

doi:10.1007/s12038-009-0025-3

Cited by 6 publications

(3 citation statements)

References 19 publications

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“…Peptides with specific affinities or activities toward targets can be screened from the peptide library. 26 − 28 Phage g3p-displayed short peptide libraries have been approved to be efficient tools for selecting mimotope peptides of an array of compounds, including metabolites of pyrethroid insecticides, 29 deoxynivalenol, 30 zearalenone, 31 ochratoxin A (OTA), 32 and aflatoxin. 33 , 34 The unique characteristics of a phage-borne peptide that connects the peptide with affinity to a target on the phage particles containing nucleic acids (single-stranded DNA) encoding the peptide make them excellent reagents to develop LAMP assays for small molecules.…”

Section: Introductionmentioning

confidence: 99%

“…Since phage peptide display was first reported, it has been a powerful tool for a variety of applications, including the isolation of peptide ligands for antibodies and enzymes, − antibody engineering, , and the isolation of receptor peptides for small molecules. , A phage display random peptide library, which displays extensive random peptides on the N terminus of the minor coat protein g3p of the filamentous phage M13, can be used for this purpose. Peptides with specific affinities or activities toward targets can be screened from the peptide library. − Phage g3p-displayed short peptide libraries have been approved to be efficient tools for selecting mimotope peptides of an array of compounds, including metabolites of pyrethroid insecticides, deoxynivalenol, zearalenone, ochratoxin A (OTA), and aflatoxin. , The unique characteristics of a phage-borne peptide that connects the peptide with affinity to a target on the phage particles containing nucleic acids (single-stranded DNA) encoding the peptide make them excellent reagents to develop LAMP assays for small molecules.…”

Section: Introductionmentioning

confidence: 99%

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Development of Phage Immuno-Loop-Mediated Isothermal Amplification Assays for Organophosphorus Pesticides in Agro-products

et al. 2014

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Two immuno-loop-mediated isothermal amplification assays (iLAMP) were developed by using a phage-borne peptide that was isolated from a cyclic eight-peptide phage library. One assay was used to screen eight organophosphorus (OP) pesticides with limits of detection (LOD) between 2 and 128 ng mL–1. The iLAMP consisted of the competitive immuno-reaction coupled to the LAMP reaction for detection. This method provides positive results in the visual color of violet, while a negative response results in a sky blue color; therefore, the iLAMP allows one to rapidly detect analytes in yes or no fashion. We validated the iLAMP by detecting parathion-methyl, parathion, and fenitrothion in Chinese cabbage, apple, and greengrocery, and the detection results were consistent with the enzyme-linked immunosorbent assay (ELISA). In conclusion, the iLAMP is a simple, rapid, sensitive, and economical method for detecting OP pesticide residues in agro-products with no instrumental requirement.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Development of Phage Immuno-Loop-Mediated Isothermal Amplification Assays for Organophosphorus Pesticides in Agro-products

et al. 2014

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“…In the melanoma model, there are few therapeutic studies using the phage-display methodology, including treatment with whole phage (13), a human melanin-binding peptide (14), and a peptide targeting a desintegrin that is important for melanoma adhesion (15). In the present work, our objective was to identify specific tumor-homing peptides by in vivo phage display and to couple it with an antiangiogenic peptide aiming at a new therapeutic approach.…”

Section: Introductionmentioning

confidence: 99%

A New Phage-Display Tumor-Homing Peptide Fused to Antiangiogenic Peptide Generates a Novel Bioactive Molecule with Antimelanoma Activity

Matsuo

Juliano

Figueiredo

et al. 2011

Molecular Cancer Research

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Phage-display peptide libraries have been widely used to identify specific peptides targeting in vivo tumor cells and the tumor vasculature and playing an important role in the discovery of antitumor bioactive peptides. In the present work, we identified a new melanoma-homing peptide, (-CVNHPAFAC-), using a C7C phage-display library directed to the developing tumor in syngeneic mice. Phage were able to preferentially target melanoma in vivo, with an affinity about 50-fold greater than that with normal tissue, and the respective synthesized peptide displaced the corresponding phage from the tumor. A preferential binding to endothelial cells rather than to melanoma cells was seen in cell ELISA, suggesting that the peptide is directed to the melanoma vasculature. Furthermore, the peptide was able to bind to human sonic hedgehog, a protein involved in the development of many types of human cancers. Using a new peptide approach therapy, we coupled the cyclic peptide to another peptide, HTMYYHHYQHHL-NH 2 , a known antagonist of VEGFR-2 receptor, using the GYG linker. The full peptide CVNHPAFACGYGHTMYYHHYQHHL-NH 2 was effective in delaying tumor growth (P < 0.05) and increasing animal survival when injected systemically, whereas a scramble-homing peptide containing the same antagonist did not have any effect. This is the first report on the synthesis of a tumor-homing peptide coupled to antiangiogenic peptide as a new anticancer therapeutics.

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Phage‐Displayed Combinatorial Peptides

Huang

Pershad

Kokoszka

et al. 2011

Amino Acids, Peptides and Proteins in Organic Chemistry

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Phage-display is a convenient vehicle for the generation and screening of combinatorial peptide libraries for a variety of purposes. With standard molecular biology techniques, it is now possible to generate phage libraries displaying 10 10 different peptides, and screen them for peptide ligands to cell surfaces, metals, and proteins, or substrates of proteases, on the time frame of weeks.The first reported display of an exogenous protein fragment on the surface of bacteriophage occurred in 1985 [1]. In pioneering work by Professor George Smith, a fragment of the b-galactosidase protein of Escherichia coli was inserted into a gene encoding a minor capsid protein of M13 bacteriophage and the resulting phage were still infectious. Not only did the resulting chimeric phage particles display epitopes of the b-galactosidase protein, but also the fusion phage could be enriched more than 1000-fold over nonrecombinant phage with antibodies to the b-galactosidase protein.Protocols were subsequently developed that permitted a single fusion phage to be isolated, through affinity selection with antibodies, from an excess of 10 8 nonrecombinant phage particles [2].Combinatorial peptide libraries that were phage-displayed appeared in three simultaneous publications in 1990. In two of the publications, the linear epitopes of two different monoclonal antibodies were mapped by affinity selecting families of related peptides from libraries of 10 8 different peptides [3,4]. In the third publication, peptide ligands to streptavidin were selected from a library of 10 8 different peptides [5]. These three publications were unique in that libraries of such a large size were available for the first time and were sufficiently large enough to represent nearly all 6-mer peptide permutations. In addition, these combinatorial peptide libraries were proposed to be the source of peptide ligands to receptors, and thus serve as agonists and antagonists. Since then, phage-displayed combinatorial peptides have been the source of peptides that selectively bind cell and tissue surfaces [6-11], cytosolic proteins [12][13][14], receptors [15][16][17][18][19][20][21], inert materials [22,23], metals [24], and toxins [25][26][27].

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Identification of binding peptides of the ADAM15 disintegrin domain using phage display

Cited by 6 publications

References 19 publications

Development of Phage Immuno-Loop-Mediated Isothermal Amplification Assays for Organophosphorus Pesticides in Agro-products

Development of Phage Immuno-Loop-Mediated Isothermal Amplification Assays for Organophosphorus Pesticides in Agro-products

A New Phage-Display Tumor-Homing Peptide Fused to Antiangiogenic Peptide Generates a Novel Bioactive Molecule with Antimelanoma Activity

Phage‐Displayed Combinatorial Peptides

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