scholarly journals Trivalent Gd-DOTA reagents for modification of proteins

RSC Advances ◽  
2015 ◽  
Vol 5 (116) ◽  
pp. 96194-96200 ◽  
Author(s):  
Martin J. Fisher ◽  
Daniel J. Williamson ◽  
George M. Burslem ◽  
Jeffrey P. Plante ◽  
Iain W. Manfield ◽  
...  

The development of novel protein-targeted MRI contrast agents crucially depends on the ability to derivatise suitable targeting moieties with a high payload of relaxation enhancer without losing affinity for the target proteins.

2014 ◽  
Vol 12 (43) ◽  
pp. 8611-8618 ◽  
Author(s):  
Shimpei Iwaki ◽  
Kazuya Hokamura ◽  
Mikako Ogawa ◽  
Yasuo Takehara ◽  
Yasuaki Muramatsu ◽  
...  

2004 ◽  
Vol 10 (20) ◽  
pp. 5205-5217 ◽  
Author(s):  
Luca Frullano ◽  
Jan Rohovec ◽  
Silvio Aime ◽  
Thomas Maschmeyer ◽  
M. Isabel Prata ◽  
...  

Author(s):  
Brigit den Adel ◽  
Mat J. Daemen ◽  
Robert E. Poelmann ◽  
Louise van der Weerd

Recent advances in molecular resonance imaging of atherosclerosis enable to visualize atherosclerotic plaques in vivo using molecular targeted contrast agents. This offers opportunities to study atherosclerosis development and plaque vulnerability noninvasively. In this review, we discuss MRI contrast agents targeted toward atherosclerotic plaques and illustrate how these new imaging platforms could assist in our understanding of atherogenesis and atheroprogression. In particular, we highlight the challenges and limitations of the different contrast agents and hurdles for clinical application. We describe the most promising existing compounds to detect atherosclerosis and plaque vulnerability. Of particular interest are the fibrin-targeted compounds that detect thrombi and, furthermore, the contrast agents targeted to integrins that allow to visualize plaque neovascularization. Moreover, vascular cell adhesion molecule 1–targeted iron oxides seem promising for early detection of atherosclerosis. These targeted MRI contrast agents, however promising and well characterized in (pre)clinical models, lack specificity for plaque vulnerability.


ChemPhysChem ◽  
2005 ◽  
Vol 6 (12) ◽  
pp. 2570-2577 ◽  
Author(s):  
Stephan G. Zech ◽  
Wei-Chuan Sun ◽  
Vincent Jacques ◽  
Peter Caravan ◽  
Andrei V. Astashkin ◽  
...  

2016 ◽  
Vol 12 (6) ◽  
pp. 1735-1745 ◽  
Author(s):  
Jennifer R. Charlton ◽  
Valeria M. Pearl ◽  
Anna R. Denotti ◽  
Jonathan B. Lee ◽  
Sundararaman Swaminathan ◽  
...  

2012 ◽  
Vol 54 (4) ◽  
pp. 454-462 ◽  
Author(s):  
Jesse L. Courtier ◽  
Emily R. Perito ◽  
Sue Rhee ◽  
Patrika Tsai ◽  
Melvin B. Heyman ◽  
...  

1988 ◽  
Vol 8 (1) ◽  
pp. 89-95 ◽  
Author(s):  
G. W. Kabalka ◽  
E. Buonocore ◽  
K. Hubner ◽  
M. Davis ◽  
L. Huang

2019 ◽  
Author(s):  
Simone Schuerle ◽  
Maiko Furubayashi ◽  
Ava P. Soleimany ◽  
Tinotenda Gwisai ◽  
Wei Huang ◽  
...  

AbstractTumor-selective contrast agents have the potential to aid in the diagnosis and treatment of cancer using noninvasive imaging modalities such as magnetic resonance imaging (MRI). Such contrast agents can consist of magnetic nanoparticles incorporating functionalities that respond to cues specific to tumor environments. Genetically engineering magnetotactic bacteria to display peptides has been investigated as a means to produce contrast agents that combine the robust image contrast effects of magnetosomes with transgenic targeting peptides displayed on their surface. This work reports the first use of magnetic nanoparticles that display genetically-encoded pH low insertion peptide (pHLIP), a long peptide intended to enhance MRI contrast by targeting the extracellular acidity associated with the tumors. To demonstrate the modularity of this versatile platform to incorporate diverse targeting ligands by genetic engineering, we also incorporated the cyclic αv integrin-binding peptide iRGD into separate magnetosomes. Specifically, we investigate their potential for enhanced binding and tumor imaging both in vitro and in vivo. Our experiments indicate that these tailored magnetosomes retain their magnetic properties, making them well-suited as T2 contrast agents, while exhibiting increased binding compared to wild-type magnetosomes.


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