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Article

An Activatable T1-Weighted MR Contrast Agent: A Noninvasive Tool for Tracking the Vicinal Thiol Motif of Thioredoxin in Live Cells

1
Research Center for Bioconvergence Analysis, Korea Basic Science Institute, Cheongju 28119, Korea
2
Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon 34134, Korea
3
Center for Research Equipment, Korea Basic Science Institute, Cheongju 28119, Korea
4
Department of Chemistry, Korea University, Seoul 02841, Korea
5
Department of Chemistry, The University of Texas at Austin, Austin, TX 78712-1224, USA
6
Centre for Interdisciplinary Sciences, JIS Institute of Advanced Studies and Research, JIS University, Kolkata 700091, India
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Carlos Geraldes
Molecules 2021, 26(7), 2018; https://doi.org/10.3390/molecules26072018
Received: 2 March 2021 / Revised: 20 March 2021 / Accepted: 22 March 2021 / Published: 1 April 2021
(This article belongs to the Special Issue Supramolecular Anion Binding and Molecular Recognition)
We have synthesized new magnetic resonance imaging (MRI) T1 contrast agents (CA1 and CA2) that permit the activatable recognition of the cellular vicinal thiol motifs of the protein thioredoxin. The contrast agents showed MR relaxivities typical of gadolinium complexes with a single water molecule coordinated to a Gd3+ center (i.e., ~4.54 mM−1s−1) for both CA1 and CA2 at 60 MHz. The contrast agent CA1 showed a ~140% relaxivity enhancement in the presence of thioredoxin, a finding attributed to a reduction in the flexibility of the molecule after binding to thioredoxin. Support for this rationale, as opposed to one based on preferential binding, came from 1H-15N-HSQC NMR spectral studies; these revealed that the binding affinities toward thioredoxin were almost the same for both CA1 and CA2. In the case of CA1, T1-weighted phantom images of cancer cells (MCF-7, A549) could be generated based on the expression of thioredoxin. We further confirmed thioredoxin expression-dependent changes in the T1-weighted contrast via knockdown of the expression of the thioredoxin using siRNA-transfected MCF-7 cells. The nontoxic nature of CA1, coupled with its relaxivity features, leads us to suggest that it constitutes a first-in-class MRI T1 contrast agent that allows for the facile and noninvasive monitoring of vicinal thiol protein motif expression in live cells. View Full-Text
Keywords: MR relaxivity; activatable contrast; thioredoxin; vicinal thiols MR relaxivity; activatable contrast; thioredoxin; vicinal thiols
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MDPI and ACS Style

Kang, J.; Hwang, E.; Lee, H.; Cho, M.Y.; Karan, S.; Kim, H.N.; Kim, J.S.; Sessler, J.L.; Bhuniya, S.; Hong, K.S. An Activatable T1-Weighted MR Contrast Agent: A Noninvasive Tool for Tracking the Vicinal Thiol Motif of Thioredoxin in Live Cells. Molecules 2021, 26, 2018. https://doi.org/10.3390/molecules26072018

AMA Style

Kang J, Hwang E, Lee H, Cho MY, Karan S, Kim HN, Kim JS, Sessler JL, Bhuniya S, Hong KS. An Activatable T1-Weighted MR Contrast Agent: A Noninvasive Tool for Tracking the Vicinal Thiol Motif of Thioredoxin in Live Cells. Molecules. 2021; 26(7):2018. https://doi.org/10.3390/molecules26072018

Chicago/Turabian Style

Kang, Jongeun, Eunha Hwang, Hyunseung Lee, Mi Young Cho, Sanu Karan, Hak Nam Kim, Jong Seung Kim, Jonathan L. Sessler, Sankarprasad Bhuniya, and Kwan Soo Hong. 2021. "An Activatable T1-Weighted MR Contrast Agent: A Noninvasive Tool for Tracking the Vicinal Thiol Motif of Thioredoxin in Live Cells" Molecules 26, no. 7: 2018. https://doi.org/10.3390/molecules26072018

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