Identification and refinement of a peptide affinity ligand with unique specificity for a monoclonal anti-tenascin-C antibody by screening of a phage display library

Bellofiore, Piero; Petronzelli, Fiorella; Martino, Tiziana; Minenkova, Olga; Bombardi, Valentina; Anastasi, Anna Maria; Lindstedt, Ragnar; Felici, Franco; Santis, Rita De; Verdoliva, Antonio

doi:10.1016/j.chroma.2005.12.064

Cited by 19 publications

(6 citation statements)

References 45 publications

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“…By using phage display, several different research groups have developed peptides with affinity for IgG molecules. Also here, peptides with affinity for the antigen binding part of IgG have been enriched [30,32]. By sequence comparison between the selected peptides and protein A, Erlich et al were able to conclude that the newly selected peptides showed homology with protein A.…”

Section: Spa Mimicsmentioning

confidence: 99%

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Protein A chromatography for antibody purification

Hober

Nord

Linhult³

2007

Journal of Chromatography B

468

330

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Section: Spa Mimicsmentioning

confidence: 99%

“…Peptides specific for a certain antibody showing affinity to the antigen binding part have been developed [30,31]. Furthermore, peptides that mimic the interaction between protein A and the Fc part of the IgG have been generated by selection [32][33][34][35].…”

Section: Spa Mimicsmentioning

confidence: 99%

Protein A chromatography for antibody purification

Hober

Nord

Linhult³

2007

Journal of Chromatography B

468

330

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“…However, it is both desirable and to be expected that novel robust protein-specific affinity reagents, generated by rapid and cost-effective manners, will gain Phage-displayed peptides Identification of peptide affinity ligand for Anti-tenascin -C Ab Competitive ELISA [40] Phage-displayed multivalent avimer proteins Antibody mimics with potential therapeutic application Indirect ELISA (for specificity analysis) [34] ScFv antibody phage-library based on chicken V genes Selection of ScFv recognising haptens, proteins and virus Indirect, sandwich and competitive ELISAs [45] Phage-displayed Fab fragments Selection of high-affinity Abs against human kallikrei tissue 1 increasing importance in proteome analysis. Antibody-based proteomics is nowadays the most powerful approach for the study of the human proteome.…”

Section: Discussionmentioning

confidence: 99%

“…These include the expression and selection of peptides binding to antibody epitopes [38][39][40], the selection of peptides for protein purification [41,42], the expression and affinity maturation of proteins, as, for example, multivalent avimer proteins, a class of binding proteins evolved from a large family of human extracellular receptor domains (human A-domains) with high therapeutic potential [34], and the selection of specific antibodies from large naïve, immune libraries or synthetic libraries [43][44][45]. Phage display has been applied in many fields of biological and medical sciences, and used to generate biological combinatorial libraries of different sizes.…”

Section: Biological Combinatorial Librariesmentioning

confidence: 99%

Immunoassays: Biological Tools for High Throughput Screening and Characterisation of Combinatorial Libraries

Taipa

2008

CCHTS

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In the demanding field of proteomics, there is an urgent need for affinity-catcher molecules to implement effective and high throughput methods for analysing the human proteome or parts of it. Antibodies have an essential role in this endeavour, and selection, isolation and characterisation of specific antibodies represent a key issue to meet success. Alternatively, it is expected that new, well-characterised affinity reagents generated in rapid and cost-effective manners will also be used to facilitate the deciphering of the function, location and interactions of the high number of encoded protein products. Combinatorial approaches combined with high throughput screening (HTS) technologies have become essential for the generation and identification of robust affinity reagents from biological combinatorial libraries and the lead discovery of active/mimic molecules in large chemical libraries. Phage and yeast display provide the means for engineering a multitude of antibody-like molecules against any desired antigen. The construction of peptide libraries is commonly used for the identification and characterisation of ligand-receptor specific interactions, and the search for novel ligands for protein purification. Further improvement of chemical and biological resistance of affinity ligands encouraged the "intelligent" design and synthesis of chemical libraries of low-molecular-weight bio-inspired mimic compounds. No matter what the ligand source, selection and characterisation of leads is a most relevant task. Immunological assays, in microtiter plates, biosensors or microarrays, are a biological tool of inestimable value for the iterative screening of combinatorial ligand libraries for tailored specificities, and improved affinities. Particularly, enzyme-linked immunosorbent assays are frequently the method of choice in a large number of screening strategies, for both biological and chemical libraries.

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“…For that reason, a TNC-specific monoclonal antibody is already in clinical trials (Akabani et al, 2005;Reardon et al, 2002) and the refinement of monoclonal anti-TNC antibodies is under study (Bellofiore et al, 2006). In addition, RNA aptamers have been developed for tumor imaging (Hicke et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

Selection and Characterization of Tenascin C Targeting Peptide

Kim

Choi

et al. 2012

Molecules and Cells

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Since tenascin C is a factor expressed highly in the tumorassociated matrix, it would be a desirable first step for targeting the tumor-specific microenvironment. In fact, a high level of tenascin C expression has been reported in most solid tumors, including lung cancer, colon cancer and glioblastoma. Therefore, the targeted binding of tenascin C in tumor stroma would inhibit tumor metastasis by modulating cancer cell growth and migration. We isolated a peptide that bound to tenascin C by phage display peptide library selection, and the selected peptide specifically recognized tenascin C protein in xenograft mouse tissue. We also observed exclusive staining of tenascin C by the selected peptide in tumor patient tissues. Moreover, the peptide reduced tenascin C-induced cell rounding and migration. We propose that the tenascin C targeting peptide may be useful as a specific anti-cancer diagnostic and therapeutic tool for most human solid tumors.

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Identification and refinement of a peptide affinity ligand with unique specificity for a monoclonal anti-tenascin-C antibody by screening of a phage display library

Cited by 19 publications

References 45 publications

Protein A chromatography for antibody purification

Protein A chromatography for antibody purification

Immunoassays: Biological Tools for High Throughput Screening and Characterisation of Combinatorial Libraries

Selection and Characterization of Tenascin C Targeting Peptide

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