scholarly journals Functionalized Carbon Nano-onions as Imaging Probes for Cancer Cells

Author(s):  
Silvia Giordani ◽  
Marco Frasconi ◽  
Roberto Marotta
Keyword(s):  
2016 ◽  
Vol 104 (11) ◽  
pp. 2854-2860 ◽  
Author(s):  
Bo Cai ◽  
Lang Rao ◽  
Xinghu Ji ◽  
Lin-Lin Bu ◽  
Zhaobo He ◽  
...  

2021 ◽  
Vol 2021 ◽  
pp. 1-10
Author(s):  
Milad Yousefvand ◽  
Zahra Mohammadi ◽  
Farzaneh Ghorbani ◽  
Rasoul Irajirad ◽  
Hormoz Abedi ◽  
...  

In recent years, the conjugation of superparamagnetic iron oxide nanoparticles (SPIONs), as tumor-imaging probes for magnetic resonance imaging (MRI), with tumor targeting peptides possesses promising advantages for specific delivery of MRI agents. The objective of the current study was to design a targeted contrast agent for MRI based on Fe3O4 nanoparticles conjugated triptorelin (SPION@triptorelin), which has a great affinity to the GnRH receptors. The SPIONs-coated carboxymethyl dextran (SPION@CMD) conjugated triptorelin (SPION@CMD@triptorelin) were synthesized using coprecipitation method and characterized by DLS, TEM, XRD, FTIR, Zeta, and VSM techniques. The relaxivities of synthetized formulations were then calculated using a 1.5 Tesla clinical magnetic field. MRI, quantitative cellular uptake, and cytotoxicity level of them were estimated. The characterization results confirmed that the formation of SPION@CMD@triptorelin has been conjugated with a suitable size. Our results demonstrated the lack of cellular cytotoxicity of SPION@CMD@triptorelin, and it could increase the cellular uptake of SPIONs to MDA-MB-231 cancer cells 6.50-fold greater than to SPION@CMD at the concentration of 75 μM. The relaxivity calculations for SPION@CMD@triptorelin showed a suitable r2 and r2/r1 with values of 31.75 mM−1·s−1 and 10.26, respectively. Our findings confirm that triptorelin-targeted SPIONs could provide a T2-weighted probe contrast agent that has the great potential for the diagnosis of GnRH-positive cancer in MRI.


2016 ◽  
Vol 14 (22) ◽  
pp. 5001-5006 ◽  
Author(s):  
Peggy R. Bohländer ◽  
Mohammed L. Abba ◽  
Felix Bestvater ◽  
Heike Allgayer ◽  
Hans-Achim Wagenknecht

Two molecular beacons were designed as complementary fluorescent imaging probes for miRNA-21 and miRNA-31.


2015 ◽  
Vol 21 (52) ◽  
pp. 19071-19080 ◽  
Author(s):  
Marco Frasconi ◽  
Roberto Marotta ◽  
Lyn Markey ◽  
Kevin Flavin ◽  
Valentina Spampinato ◽  
...  
Keyword(s):  

2019 ◽  
Vol 58 (18) ◽  
pp. 12422-12432 ◽  
Author(s):  
Johannes Karges ◽  
Olivier Blacque ◽  
Hui Chao ◽  
Gilles Gasser
Keyword(s):  

2017 ◽  
Vol 8 (6) ◽  
pp. 4634-4643 ◽  
Author(s):  
Alexander Nicol ◽  
Wei Qin ◽  
Ryan T. K. Kwok ◽  
Jeffrey Mark Burkhartsmeyer ◽  
Zhenfeng Zhu ◽  
...  

Mitochondria targeting biotinylated AIE nanoparticles are used as multiphoton imaging probes to identify cancer cells.


2016 ◽  
Vol 17 (7) ◽  
pp. 1086 ◽  
Author(s):  
Haruka Yamaguchi ◽  
Makoto Tsuchimochi ◽  
Kazuhide Hayama ◽  
Tomoyuki Kawase ◽  
Norio Tsubokawa

2021 ◽  
Vol 12 (1) ◽  
pp. 2-24

The incidence of cancer in the world is growing steadily. Therefore, it is necessary to develop new approaches for the early diagnosis of cancer. This work is devoted to the study of the potential of RHAMM-target peptides for molecular diagnosis of cancer. The key amino acids of the RHAMM target peptides were identified by the alanine scan method. The specificity of binding of peptides to RHAMM-CT was assessed using competitive HA substitution by the ELISA method. RHAMM-CT was obtained by genetic engineering and isolated by affinity chromatography. The interaction of RHAMM target peptides with the surface receptor of tumor cells was evaluated by confocal microscopy. It has been shown that fragment EEGEEZ in the peptides' composition is necessary for binding to the RHAMM-CT. The results showed that the RHAMM-target peptides bind specifically to the RHAMM-CT and competitively substituted HA at the RHAMM. It has been found that aggrecan is unable to displace peptides from the HA binding site of RHAMM-CT. The results showed that the FITC peptide binds specifically to RHAMM on the surface of prostate cancer cells. Therefore, RHAMM-target peptides have the potential for early molecular diagnosis of cancer.


2014 ◽  
Vol 50 (98) ◽  
pp. 15503-15505 ◽  
Author(s):  
Laura H. Davies ◽  
Benjamin B. Kasten ◽  
Paul D. Benny ◽  
Rory L. Arrowsmith ◽  
Haobo Ge ◽  
...  

A fluorescent tridentate phosphine, BodP3(2), forms rhenium complexes which effectively image cancer cells.


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