Related Experiment Video
Updated: Jul 14, 2026
Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library
Published on: September 30, 2019
Identification and evaluation of a new tumor cell-binding peptide, FROP-1
Sabine Zitzmann1, Susanne Krämer, Walter Mier
1Clinical Cooperation Unit Nuclear Medicine, German Cancer Research Center, Heidelberg, Germany. sabine.zitzmann@schering.de
Unlabelled:
Peptides are useful tools for the targeted delivery of radionuclides or chemotherapeutic drugs to their site of action within an organism. Given that the peptide receptor is overexpressed at the tumor, therapeutically active doses can be delivered to the tumor with reduced side effects. Because currently known peptides are restricted to a small number of tumors, new molecules and their corresponding receptors have to be identified to enlarge the spectrum of malignancies that can be diagnosed or treated using tumor-targeting peptides.
Methods:
A 12-amino-acid peptide phage display system was applied to identify a new peptide binding to follicular thyroid carcinoma cells. The properties of the radiolabeled peptide were assessed in binding, competition, and internalization experiments in a variety of tumor cell lines including FRO82-2 and MCF-7 cells, and the pharmacokinetic behavior of the radiolabeled peptide was evaluated in tumor-bearing mice. Peptide stability was studied in human serum.
Results:
After 5 selection rounds, the new peptide, FROP-1 (EDYELMDLLAYL), was identified. It showed binding to follicular thyroid carcinoma as well as anaplastic thyroid carcinoma, mammary carcinoma, cervix carcinoma, prostate carcinoma, and cell lines derived from head and neck tumors, and low affinity could be observed to control cells such as human umbilical vein endothelial cells or immortalized keratinocytes. In MCF7 cells, 78% and 86% of the bound activity was internalized after 10 and 60 min of incubation, respectively. Stability experiments in human serum showed the appearance of a degradation product after 15 min. Tumor uptake of the radioactive labeled peptide increased for 45 min in nude mouse models, reaching an accumulation level of approximately 3.6 percentage injected dose (%ID)/g for FRO82-2 tumors or approximately 3.8 %ID/g for MCF-7 tumors.
Conclusion:
The target of FROP-1 is most likely a molecule found generally in tumors, making this peptide highly attractive for diagnostic or therapeutic applications. However, modifications are needed to increase stability and affinity.
Insights
Researchers identified a new peptide, FROP-1, that targets various cancer cells, including thyroid and breast tumors. This peptide shows promise for targeted cancer diagnosis and therapy, though modifications are needed to enhance its stability and binding affinity.
Area of Science:
- Oncology
- Molecular Biology
- Drug Discovery
Background:
- Peptides facilitate targeted delivery of therapeutics to tumors.
- Overexpressed peptide receptors on tumors enable localized drug delivery, minimizing side effects.
- Current peptide limitations necessitate identification of new molecules for broader cancer treatment.
Purpose of the Study:
- To identify novel peptides for targeting cancer cells.
- To evaluate the potential of newly identified peptides in cancer diagnostics and therapeutics.
Main Methods:
- A 12-amino-acid peptide phage display system was employed.
- The novel peptide FROP-1 was identified and characterized.
- Binding, competition, internalization, stability, and pharmacokinetic studies were performed using various cancer cell lines and tumor-bearing mice.
Main Results:
- The peptide FROP-1 demonstrated binding to multiple cancer cell lines, including follicular thyroid, anaplastic thyroid, mammary, cervix, prostate, and head and neck tumors.
- FROP-1 showed high internalization rates in MCF7 cells (78% at 10 min, 86% at 60 min).
- In vivo studies revealed significant tumor uptake in mouse models, with approximately 3.6-3.8 %ID/g in FRO82-2 and MCF-7 tumors.
Conclusions:
- FROP-1 shows potential for broad application in cancer diagnostics and therapeutics due to its likely general tumor target.
- Further modifications are required to improve FROP-1's stability and binding affinity for clinical use.
More Related Videos
![Automated Preparation of [68Ga]Ga-3BP-3940 on a Synthesis Module for PET Imaging of the Tumor Microenvironment](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F68356.jpg&w=3840&q=50)
10:33Automated Preparation of [68Ga]Ga-3BP-3940 on a Synthesis Module for PET Imaging of the Tumor Microenvironment
Published on: April 25, 2025
10:46A Flow Cytometry-Based Cell Surface Protein Binding Assay for Assessing Selectivity and Specificity of an Anticancer Aptamer
Published on: September 13, 2022