ArticleJournal of protein chemistry2003
Combinatorial evolution of high-affinity peptides that bind to the Thomsen-Friedenreich carcinoma antigen.
Article in Journal of protein chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 36 citations in OpenAlex.
- Review
- Phage Display Selection, Identification, and Characterization of Novel Pancreatic Cancer Targeting Peptides.Biomolecules · 2020Article
- High-Throughput Approaches to the Development of Molecular Imaging Agents.Molecular imaging and biology · 2017Review
- Tumor-targeting peptides from combinatorial libraries.Advanced drug delivery reviews · 2017Review
- Multiple Bacteriophage Selection Strategies for Improved Affinity of a Peptide Targeting ERBB2.International journal of peptide research and therapeutics · 2015Article
- Affinity maturation of an ERBB2-targeted SPECT imaging peptide by in vivo phage display.Molecular imaging and biology · 2014Article
- Combinatorial peptide libraries: mining for cell-binding peptides.Chemical reviews · 2014Review
- Phage display--a powerful technique for immunotherapy: 1. Introduction and potential of therapeutic applications.Human vaccines & immunotherapeutics · 2012Review
- Phage display in molecular imaging and diagnosis of cancer.Chemical reviews · 2010Review
- Progress in biomimetic carbohydrate recognition.Cellular and molecular life sciences : CMLS · 2009Review
- In vivo selection of phage for the optical imaging of PC-3 human prostate carcinoma in mice.Neoplasia (New York, N.Y.) · 2006Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thomsen-Friedenreich (TF) antigen occurs on approximately 90% of human carcinomas, is likely involved in carcinoma cell homotypic aggregation, and has clinical value as a prognostic indicator and marker of metastasized cells. Previously, we isolated anti-TF antigen peptides from bacteriophage display libraries. These bound to TF antigen on carcinoma cells but were of low affinity and solubility. We hypothesized that peptide amino acid sequence changes would result in increased affinity and solubility, which would translate into improved carcinoma cell binding and increased inhibition of aggregation. The new peptides were more soluble and exhibited up to fivefold increase in affinity (Kd approximately equal to 60 nM). They bound cultured human breast and prostate carcinoma cells at low concentrations, whereas the earlier peptides did not. Moreover, the new peptides were potent inhibitors of homotypic aggregation. The maturated peptides will have expanded applications in basic studies of the TF antigen and particular utility as clinical carcinoma-targeting agents.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.