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Related Experiment Video

Updated: Mar 23, 2026

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

Published on: September 30, 2019

Switchable probes: pH-triggered and VEGFR2 targeted peptides screening through imprinting microarray.

Yixia Qian¹, Weizhi Wang², Zihua Wang²

¹CAS Center for Excellence in Nanoscience, National Center for Nanoscience and Technology, Beijing 100190, China. wangwz@nanoctr.cn huzy@nanoctr.cn and University of Chinese Academy of Science, No. 19A Yuquan Road, Beijing 100049, China and Sino-Danish Center for Education and Research, Beijing, 100190, China.

Chemical Communications (Cambridge, England)

|April 2, 2016

Summary

This summary is machine-generated.

A novel switchable affinity peptide (STP) enables targeted cell imaging by responding to VEGFR2 overexpression and acidic conditions. This peptide enhances cell recognition and penetration for accelerated in vivo imaging.

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Last Updated: Mar 23, 2026

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

Published on: September 30, 2019

Screening Peptides that Activate MRGPRX2 using Engineered HEK Cells

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Published on: November 6, 2021

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Area of Science:

Biomaterials Science
Molecular Imaging
Biotechnology

Background:

Developing targeted probes for molecular imaging is crucial for disease diagnosis.
Switchable affinity molecules offer potential for controlled biological interactions.
Vascular Endothelial Growth Factor Receptor 2 (VEGFR2) is a key target in various diseases.

Purpose of the Study:

To screen and characterize a switchable affinity peptide (STP) for targeted molecular imaging.
To investigate the pH-triggered and VEGFR2-dependent functionality of STP.
To evaluate the efficacy of STP in cell recognition, penetration, and in vivo imaging.

Main Methods:

High-throughput screening using an integrated imprinting microarray to identify STP.
Characterization of STP's binding affinity and pH-dependent behavior.
In vitro cell-based assays for recognition and penetration studies.
In vivo imaging experiments in relevant models.

Main Results:

STP was successfully screened and identified as a pH-triggered ligand for VEGFR2.
STP demonstrated efficient cell recognition and penetration capabilities.
In vivo imaging signal was effectively 'turned on' and accelerated under conditions of VEGFR2 overexpression and mild acidity.
The peptide's performance was contingent on both target overexpression and environmental pH.

Conclusions:

STP represents a novel switchable affinity peptide with potential for targeted molecular imaging.
The dual-triggering mechanism (VEGFR2 and pH) allows for precise control over imaging probe activation.
STP facilitates accelerated and efficient in vivo imaging in specific pathological microenvironments.