IMR Press / FBL / Volume 13 / Issue 5 / DOI: 10.2741/2795

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Site-specifically modified fusion proteins for molecular imaging
Show Less
1 The Molecular Imaging Program at Stanford (MIPS), Department of Radiology and Bio-X Program, Stanford University School of Medicine, Stanford, California

Academic Editor: Xiaoyuan Chen

Front. Biosci. (Landmark Ed) 2008, 13(5), 1716–1732;
Published: 1 January 2008
(This article belongs to the Special Issue Molecular imaging of biomarkers)

To visualize and quantify specific molecular pathways in vivo, it is essential to develop molecular imaging probes with high target affinity and specificity. The introduction of radioisotope, fluorophores and other detectable labels onto a protein ligand in a site-specific manner without compromising its function and binding affinity has been a valuable tool for such molecular imaging. Site-specific labeling of proteins poses an enormous challenge, because the correct functional groups of one protein amidst all of the other expressed proteins containing the same range of amino acids must be accurately targeted. Chemists have developed many diverse strategies for accomplishing sit-specific modification; unnatural amino acids have been incorporated into targeted protein for site-specific modification. Enzymatic post-translational modification of proteins is an alternative approach and beneficial complement for site-specific labeling. A small peptide tag is a substrate for the enzyme that can be appended to N-, C-terminus or internal of target protein for site-specific labeling. In this review, we will discuss several valuable tags for addressing this problem, and comment on the potential usage of tagged fusion protein for molecular imaging.

Back to top