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Journal articles on the topic 'Paramagnetic lanthanide binding tags'

Author: Grafiati

Published: 11 December 2022

Last updated: 25 January 2023

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1

Lee, M. D., C. T. Loh, J. Shin, S. Chhabra, M. L. Dennis, G. Otting, J. D. Swarbrick, and B. Graham. "Compact, hydrophilic, lanthanide-binding tags for paramagnetic NMR spectroscopy." Chemical Science 6, no. 4 (2015): 2614–24. http://dx.doi.org/10.1039/c4sc03892d.

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2

Lee, Michael D., Matthew L. Dennis, Bim Graham, and James D. Swarbrick. "Short two-armed lanthanide-binding tags for paramagnetic NMR spectroscopy based on chiral 1,4,7,10-tetrakis(2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane scaffolds." Chemical Communications 53, no. 99 (2017): 13205–8. http://dx.doi.org/10.1039/c7cc07961c.

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3

Lee, Michael D., Matthew L. Dennis, James D. Swarbrick, and Bim Graham. "Enantiomeric two-armed lanthanide-binding tags for complementary effects in paramagnetic NMR spectroscopy." Chemical Communications 52, no. 51 (2016): 7954–57. http://dx.doi.org/10.1039/c6cc02325h.

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4

Chen, Jia-Liang, Ben-Guang Chen, Bin Li, Feng Yang, and Xun-Cheng Su. "Assessing multiple conformations of lanthanide binding tags for proteins using a sensitive 19F-reporter." Chemical Communications 57, no. 35 (2021): 4291–94. http://dx.doi.org/10.1039/d1cc00791b.

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¹⁹F is an efficient reporter in quantifying the individual isomers and assessing the dynamic exchange between the isomers for the lanthanide complexes. ¹⁹F-NMR is a valuable tool in the design of suitable paramagnetic tags for protein NMR analysis.

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5

Orton, Henry W., Iresha D. Herath, Ansis Maleckis, Shereen Jabar, Monika Szabo, Bim Graham, Colum Breen, Lydia Topping, Stephen J. Butler, and Gottfried Otting. "Localising individual atoms of tryptophan side chains in the metallo-<i>β</i>-lactamase IMP-1 by pseudocontact shifts from paramagnetic lanthanoid tags at multiple sites." Magnetic Resonance 3, no. 1 (January 4, 2022): 1–13. http://dx.doi.org/10.5194/mr-3-1-2022.

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Abstract. The metallo-β-lactamase IMP-1 features a flexible loop near the active site that assumes different conformations in single crystal structures, which may assist in substrate binding and enzymatic activity. To probe the position of this loop, we labelled the tryptophan residues of IMP-1 with 7-13C-indole and the protein with lanthanoid tags at three different sites. The magnetic susceptibility anisotropy (Δχ) tensors were determined by measuring pseudocontact shifts (PCSs) of backbone amide protons. The Δχ tensors were subsequently used to identify the atomic coordinates of the tryptophan side chains in the protein. The PCSs were sufficient to determine the location of Trp28, which is in the active site loop targeted by our experiments, with high accuracy. Its average atomic coordinates showed barely significant changes in response to the inhibitor captopril. It was found that localisation spaces could be defined with better accuracy by including only the PCSs of a single paramagnetic lanthanoid ion for each tag and tagging site. The effect was attributed to the shallow angle with which PCS isosurfaces tend to intersect if generated by tags and tagging sites that are identical except for the paramagnetic lanthanoid ion.

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6

Sandtner, Walter, Bernhard Egwolf, Benoit Roux, Ana M. Correa, and Francisco Bezanilla. "Optical force measurements utilizing Lanthanide Binding Tags." Biophysical Journal 96, no. 3 (February 2009): 402a—403a. http://dx.doi.org/10.1016/j.bpj.2008.12.2048.

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7

Franz, Katherine J., Mark Nitz, and Barbara Imperiali. "Lanthanide-Binding Tags as Versatile Protein Coexpression Probes." ChemBioChem 4, no. 4 (March 26, 2003): 265–71. http://dx.doi.org/10.1002/cbic.200390046.

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8

Silvaggi, Nicholas R., Langdon J. Martin, Harald Schwalbe, Barbara Imperiali, and Karen N. Allen. "Double-Lanthanide-Binding Tags for Macromolecular Crystallographic Structure Determination." Journal of the American Chemical Society 129, no. 22 (June 2007): 7114–20. http://dx.doi.org/10.1021/ja070481n.

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9

Daughtry, Kelly D., Langdon J. Martin, Ashish Sarraju, Barbara Imperiali, and Karen N. Allen. "Tailoring Encodable Lanthanide-Binding Tags as MRI Contrast Agents." ChemBioChem 13, no. 17 (November 13, 2012): 2567–74. http://dx.doi.org/10.1002/cbic.201200448.

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10

Mallagaray, Alvaro, Gema Domínguez, Thomas Peters, and Javier Pérez-Castells. "A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus." Chemical Communications 52, no. 3 (2016): 601–4. http://dx.doi.org/10.1039/c5cc05827a.

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11

Barthelmes, Katja, Anne M. Reynolds, Ezra Peisach, Hendrik R. A. Jonker, Nicholas J. DeNunzio, Karen N. Allen, Barbara Imperiali, and Harald Schwalbe. "Engineering Encodable Lanthanide-Binding Tags into Loop Regions of Proteins." Journal of the American Chemical Society 133, no. 4 (February 2, 2011): 808–19. http://dx.doi.org/10.1021/ja104983t.

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12

Martin, Langdon J., Martin J. Hähnke, Mark Nitz, Jens Wöhnert, Nicholas R. Silvaggi, Karen N. Allen, Harald Schwalbe, and Barbara Imperiali. "Double-Lanthanide-Binding Tags: Design, Photophysical Properties, and NMR Applications." Journal of the American Chemical Society 129, no. 22 (June 2007): 7106–13. http://dx.doi.org/10.1021/ja070480v.

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13

Sculimbrene, Bianca R., and Barbara Imperiali. "Lanthanide-Binding Tags as Luminescent Probes for Studying Protein Interactions." Journal of the American Chemical Society 128, no. 22 (June 2006): 7346–52. http://dx.doi.org/10.1021/ja061188a.

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14

Mekkattu Tharayil, Sreelakshmi, Mithun Chamikara Mahawaththa, Choy-Theng Loh, Ibidolapo Adekoya, and Gottfried Otting. "Phosphoserine for the generation of lanthanide-binding sites on proteins for paramagnetic nuclear magnetic resonance spectroscopy." Magnetic Resonance 2, no. 1 (January 6, 2021): 1–13. http://dx.doi.org/10.5194/mr-2-1-2021.

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Abstract. Pseudocontact shifts (PCSs) generated by paramagnetic lanthanide ions provide valuable long-range structural information in nuclear magnetic resonance (NMR) spectroscopic analyses of biological macromolecules such as proteins, but labelling proteins site-specifically with a single lanthanide ion remains an ongoing challenge, especially for proteins that are not suitable for ligation with cysteine-reactive lanthanide complexes. We show that a specific lanthanide-binding site can be installed on proteins by incorporation of phosphoserine in conjunction with other negatively charged residues, such as aspartate, glutamate or a second phosphoserine residue. The close proximity of the binding sites to the protein backbone leads to good immobilization of the lanthanide ion, as evidenced by the excellent quality of fits between experimental PCSs and PCSs calculated with a single magnetic susceptibility anisotropy (Δχ) tensor. An improved two-plasmid system was designed to enhance the yields of proteins with genetically encoded phosphoserine, and good lanthanide ion affinities were obtained when the side chains of the phosphoserine and aspartate residues are not engaged in salt bridges, although the presence of too many negatively charged residues in close proximity can also lead to unfolding of the protein. In view of the quality of the Δχ tensors that can be obtained from lanthanide-binding sites generated by site-specific incorporation of phosphoserine, this method presents an attractive tool for generating PCSs in stable proteins, particularly as it is independent of cysteine residues.

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15

Park, Dan M., David W. Reed, Mimi C. Yung, Ali Eslamimanesh, Malgorzata M. Lencka, Andrzej Anderko, Yoshiko Fujita, Richard E. Riman, Alexandra Navrotsky, and Yongqin Jiao. "Bioadsorption of Rare Earth Elements through Cell Surface Display of Lanthanide Binding Tags." Environmental Science & Technology 50, no. 5 (February 16, 2016): 2735–42. http://dx.doi.org/10.1021/acs.est.5b06129.

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16

Abdelkader, Elwy H., Xuejun Yao, Akiva Feintuch, Luke A. Adams, Luigi Aurelio, Bim Graham, Daniella Goldfarb, and Gottfried Otting. "Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags." Journal of Biomolecular NMR 64, no. 1 (November 23, 2015): 39–51. http://dx.doi.org/10.1007/s10858-015-0003-z.

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17

Swarbrick, James D., Phuc Ung, Sandeep Chhabra, and Bim Graham. "An Iminodiacetic Acid Based Lanthanide Binding Tag for Paramagnetic Exchange NMR Spectroscopy." Angewandte Chemie International Edition 50, no. 19 (April 7, 2011): 4403–6. http://dx.doi.org/10.1002/anie.201007221.

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18

Swarbrick, James D., Phuc Ung, Sandeep Chhabra, and Bim Graham. "An Iminodiacetic Acid Based Lanthanide Binding Tag for Paramagnetic Exchange NMR Spectroscopy." Angewandte Chemie 123, no. 19 (April 7, 2011): 4495–98. http://dx.doi.org/10.1002/ange.201007221.

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19

Blackburn, Octavia A., Alan M. Kenwright, Paul D. Beer, and Stephen Faulkner. "Axial fluoride binding by lanthanide DTMA complexes alters the local crystal field, resulting in dramatic spectroscopic changes." Dalton Transactions 44, no. 45 (2015): 19509–17. http://dx.doi.org/10.1039/c5dt02398j.

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Dramatic changes are observed in both the NMR and luminescence spectra of LnDTMA complexes on addition of fluoride, consistent with a change in the nature of the magnetic anisotropy at the paramagnetic lanthanide centre.

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20

Pan, Bin-Bin, Feng Yang, Yansheng Ye, Qiong Wu, Conggang Li, Thomas Huber, and Xun-Cheng Su. "3D structure determination of a protein in living cells using paramagnetic NMR spectroscopy." Chemical Communications 52, no. 67 (2016): 10237–40. http://dx.doi.org/10.1039/c6cc05490k.

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The integration of site-specific labeling of proteins with a stable lanthanide binding tag, paramagnetic NMR spectroscopy and the GPS-Rosetta program presents an effective and fast way of determining the three-dimensional structure of a protein in living cells.

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21

Martin, Langdon J, Bianca R Sculimbrene, Mark Nitz, and Barbara Imperiali. "Rapid Combinatorial Screening of Peptide Libraries for the Selection of Lanthanide-Binding Tags (LBTs)." QSAR & Combinatorial Science 24, no. 10 (December 2005): 1149–57. http://dx.doi.org/10.1002/qsar.200540007.

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22

Prosser, R. Scott, V. B. Volkov, and I. V. Shiyanovskaya. "Solid-state NMR studies of magnetically aligned phospholipid membranes: taming lanthanides for membrane protein studies." Biochemistry and Cell Biology 76, no. 2-3 (May 1, 1998): 443–51. http://dx.doi.org/10.1139/o98-058.

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The addition of lanthanides (Tm3+, Yb3+, Er3+, or Eu3+) to a solution of long-chain phospholipids such as dimyristoylphosphatidylcholine (DMPC) and short-chain phospholipids such as dihexanoylphosphatidylcholine (DHPC) is known to result in a bilayer phase in which the average bilayer normal aligns parallel to an applied magnetic field. Lanthanide-doped bilayers have enormous potential for the study of membrane proteins by solid-state NMR, low-angle diffraction, and a variety of optical spectroscopic techniques. However, the addition of lanthanides poses certain challenges to the NMR spectroscopist: coexistence of an isotropic phase and hysteresis effects, direct binding of the paramagnetic ion to the peptide or protein of interest, and severe paramagnetic shifts and line broadening. Lower water concentrations and larger DMPC/DHPC ratios than those typically used in bicelles consistently yield a single oriented bilayer phase that is stable over a wide range of temperature (~35-90°C). Among the above choice of lanthanides, Yb3+ is found to give minimal paramagnetic shifts and line broadening at acceptably low concentrations necessary for alignment (i.e., Yb3+/DMPC mole ratios equal to or greater than 0.01). Finally, the addition of a phospholipid chelate, 1,2-dimyristoyl-sn-glycero-3-phosphoethanolamine - diethylenetriaminepentaacetic acid, is observed to significantly reduce paramagnetic broadening and presumably prevent direct association of the peptide with the lanthanide ions.Key words: lanthanide, solid-state NMR, model membrane, membrane protein structure.

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23

Victor, Tiffany W., Katherine H. O’Toole, Lindsey M. Easthon, Mingyuan Ge, Randy J. Smith, Xiaojing Huang, Hanfei Yan, et al. "Lanthanide-Binding Tags for 3D X-ray Imaging of Proteins in Cells at Nanoscale Resolution." Journal of the American Chemical Society 142, no. 5 (January 10, 2020): 2145–49. http://dx.doi.org/10.1021/jacs.9b11571.

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24

Reynolds, Anne M., Bianca R. Sculimbrene, and Barbara Imperiali. "Lanthanide-Binding Tags with Unnatural Amino Acids: Sensitizing Tb3+and Eu3+Luminescence at Longer Wavelengths." Bioconjugate Chemistry 19, no. 3 (March 2008): 588–91. http://dx.doi.org/10.1021/bc700426c.

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25

Chang, Elliot, Aaron W. Brewer, Dan M. Park, Yongqin Jiao, and Laura N. Lammers. "Surface complexation model of rare earth element adsorption onto bacterial surfaces with lanthanide binding tags." Applied Geochemistry 112 (January 2020): 104478. http://dx.doi.org/10.1016/j.apgeochem.2019.104478.

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26

Barthelmes, Dominic, Katja Barthelmes, Kai Schnorr, Hendrik R. A. Jonker, Bianca Bodmer, Karen N. Allen, Barbara Imperiali, and Harald Schwalbe. "Conformational dynamics and alignment properties of loop lanthanide-binding-tags (LBTs) studied in interleukin-1β." Journal of Biomolecular NMR 68, no. 3 (May 22, 2017): 187–94. http://dx.doi.org/10.1007/s10858-017-0118-5.

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27

Rosaleny, Lorena E., and Alejandro Gaita-Ariño. "Theoretical evaluation of lanthanide binding tags as biomolecular handles for the organization of single ion magnets and spin qubits." Inorganic Chemistry Frontiers 3, no. 1 (2016): 61–66. http://dx.doi.org/10.1039/c5qi00127g.

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28

Barthelmes, Dominic, Markus Gränz, Katja Barthelmes, Karen N. Allen, Barbara Imperiali, Thomas Prisner, and Harald Schwalbe. "Encoded loop-lanthanide-binding tags for long-range distance measurements in proteins by NMR and EPR spectroscopy." Journal of Biomolecular NMR 63, no. 3 (September 4, 2015): 275–82. http://dx.doi.org/10.1007/s10858-015-9984-x.

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29

Canales, Angeles, Alvaro Mallagaray, Javier Pérez-Castells, Irene Boos, Carlo Unverzagt, Sadine André, Hans-Joachim Gabius, Francisco Javier Cañada, and Jesús Jiménez-Barbero. "Breaking Pseudo-Symmetry in Multiantennary Complex N-Glycans Using Lanthanide-Binding Tags and NMR Pseudo-Contact Shifts." Angewandte Chemie 125, no. 51 (November 4, 2013): 14034–38. http://dx.doi.org/10.1002/ange.201307845.

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30

Canales, Angeles, Alvaro Mallagaray, Javier Pérez-Castells, Irene Boos, Carlo Unverzagt, Sadine André, Hans-Joachim Gabius, Francisco Javier Cañada, and Jesús Jiménez-Barbero. "Breaking Pseudo-Symmetry in Multiantennary Complex N-Glycans Using Lanthanide-Binding Tags and NMR Pseudo-Contact Shifts." Angewandte Chemie International Edition 52, no. 51 (November 4, 2013): 13789–93. http://dx.doi.org/10.1002/anie.201307845.

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31

Teterin, Yury, Labud Vukcevic, and Anton Teterin. "Structure of X-ray photoelectron spectra of low-energy and core electrons of Ln(C6H4OCH3COO-)3." Nuclear Technology and Radiation Protection 20, no. 2 (2005): 17–22. http://dx.doi.org/10.2298/ntrp0502017t.

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This paper deals with the results of an X-ray photo electron spectroscopy of lanthanide ortho-metoxybenzoates Ln(C6H4OCH3COO-)3, where Ln represents lanthanides La through Lu except for Pm and C6H4OCH3COO- - residuum of ortho-metoxybenzoic acid. The core and outer electron X-ray photo electron spectroscopy spectra in the binding energy range of 0-1250 eV were shown to exhibit a complex, fine structure. The said structure was established due to the outer (0-15 eV binding energy) and inner (15-50 eV binding energy) valence molecular orbital from the filled Ln5p and O2s atomic shells multiple splitting, many-body perturbation, dynamic effect, etc. The mechanisms of such a fine structure formation were shown to manifest different probabilities in the spectrum of a certain electronic shell. There fore, the fine X-ray photo electron spectroscopy spectral structure resulting from a certain mechanism can be interpreted and its quantitative parameters related to the physical and chemical properties of the studied com pounds (degree of delocalization and participation of Ln4f electrons in the chemical bond, electronic configuration and oxidation states, density of uncoupled electrons on paramagnetic ions, degree of participation of the low binding energy filled electronic shells of lanthanide and ligands information of the outer and in nervalence molecular orbitals, lanthanide close environment structure in amorphous materials, etc).

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32

Su, Xun-Cheng, Kerry McAndrew, Thomas Huber, and Gottfried Otting. "Lanthanide-Binding Peptides for NMR Measurements of Residual Dipolar Couplings and Paramagnetic Effects from Multiple Angles." Journal of the American Chemical Society 130, no. 5 (February 2008): 1681–87. http://dx.doi.org/10.1021/ja076564l.

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33

Kubota, Tomoya, Thomas Durek, Bobo Dang, Rocio K. Finol-Urdaneta, David J. Craik, Stephen B. H. Kent, Robert J. French, Francisco Bezanilla, and Ana M. Correa. "Mapping of voltage sensor positions in resting and inactivated mammalian sodium channels by LRET." Proceedings of the National Academy of Sciences 114, no. 10 (February 15, 2017): E1857—E1865. http://dx.doi.org/10.1073/pnas.1700453114.

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Voltage-gated sodium channels (Navs) play crucial roles in excitable cells. Although vertebrate Nav function has been extensively studied, the detailed structural basis for voltage-dependent gating mechanisms remain obscure. We have assessed the structural changes of the Nav voltage sensor domain using lanthanide-based resonance energy transfer (LRET) between the rat skeletal muscle voltage-gated sodium channel (Nav1.4) and fluorescently labeled Nav1.4-targeting toxins. We generated donor constructs with genetically encoded lanthanide-binding tags (LBTs) inserted at the extracellular end of the S4 segment of each domain (with a single LBT per construct). Three different Bodipy-labeled, Nav1.4-targeting toxins were synthesized as acceptors: β-scorpion toxin (Ts1)-Bodipy, KIIIA-Bodipy, and GIIIA-Bodipy analogs. Functional Nav-LBT channels expressed inXenopusoocytes were voltage-clamped, and distinct LRET signals were obtained in the resting and slow inactivated states. Intramolecular distances computed from the LRET signals define a geometrical map of Nav1.4 with the bound toxins, and reveal voltage-dependent structural changes related to channel gating.

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34

Saio, Tomohide, Kenji Ogura, Masashi Yokochi, Yoshihiro Kobashigawa, and Fuyuhiko Inagaki. "Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect." Journal of Biomolecular NMR 44, no. 3 (May 26, 2009): 157–66. http://dx.doi.org/10.1007/s10858-009-9325-z.

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35

D'Amelio, Nicola, Elena Gaggelli, Nicola Gaggelli, Francesca Mancini, Elena Molteni, Daniela Valensin, and Gianni Valensin. "Probing the role of metal ions on reversible peptide–protein interactions by NMR." Spectroscopy 18, no. 2 (2004): 251–56. http://dx.doi.org/10.1155/2004/583454.

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This work provides evidence that paramagnetic lanthanide ions constitute ideal probes suitable for investigations of metal effects upon peptide–receptor interactions with the use of NMR methods. Cerium(III) is herein used for assessing metal effects upon the interaction between angiotensin II and a fragment from the AT1Areceptor. Angiotensin II forms a complex with cerium(III) in water while the fCT300–320receptor fragment is poorly affected by cerium(III). However, the addition of the fragment displaces cerium(III) from the complex, thus directly demonstrating the higher affinity of angiotensin II for the receptor and probing the peptide residues involved in receptor binding.

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36

Kiraev, Salauat R., Emilie Mathieu, Fiona Siemens, Daniel Kovacs, Ellen Demeyere, and K. Eszter Borbas. "Lanthanide(III) Complexes of Cyclen Triacetates and Triamides Bearing Tertiary Amide-Linked Antennae." Molecules 25, no. 22 (November 12, 2020): 5282. http://dx.doi.org/10.3390/molecules25225282.

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The coordination compounds of the trivalent lanthanide ions (Ln(III)) have unique photophysical properties. Ln(III) excitation is usually performed through a light-harvesting antenna. To enable Ln(III)-based emitters to reach their full potential, an understanding of how complex structure affects sensitization and quenching processes is necessary. Here, the role of the linker between the antenna and the metal binding fragment was studied. Four macrocyclic ligands carrying coumarin 2 or 4-methoxymethylcarbostyril sensitizing antennae linked to an octadentate macrocyclic ligand binding site were synthesized. Complexation with Ln(III) (Ln = La, Sm, Eu, Gd, Tb, Yb and Lu) yielded species with overall −1, 0, or +2 and +3-charge. Paramagnetic 1H NMR spectroscopy indicated subtle differences between the coumarin- and carbostyril-carrying Eu(III) and Yb(III) complexes. Cyclic voltammetry showed that the effect of the linker on the Eu(III)/Eu(II) apparent reduction potential was dependent on the electronic properties of the N-substituent. The Eu(III), Tb(III) and Sm(III) complexes were all luminescent. Coumarin-sensitized complexes were poorly emissive; photoinduced electron transfer was not a major quenching pathway in these species. These results show that seemingly similar emitters can undergo very different photophysical processes, and highlight the crucial role the linker can play.

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37

Swarbrick, James D., Phuc Ung, Xun-Cheng Su, Ansis Maleckis, Sandeep Chhabra, Thomas Huber, Gottfried Otting, and Bim Graham. "Engineering of a bis-chelator motif into a protein α-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy." Chemical Communications 47, no. 26 (2011): 7368. http://dx.doi.org/10.1039/c1cc11893e.

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38

Cooper, Tamara, Wayne R. Leifert, Richard V. Glatz, and Edward J. McMurchie. "Expression and Characterisation of Functional Lanthanide-Binding Tags Fused to a Gα-Protein and Muscarinic (M₂) Receptor." Journal of Bionanoscience 2, no. 1 (June 1, 2008): 27–34. http://dx.doi.org/10.1166/jbns.2008.023.

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39

Mukidjam, Elizabeth, Stephen Barnes, and Gabriel A. Elgavish. "NMR studies of the binding of sodium and calcium ions to the bile salts glycocholate and taurocholate in dilute solution, as probed by the paramagnetic lanthanide dysprosium." Journal of the American Chemical Society 108, no. 22 (October 1986): 7082–89. http://dx.doi.org/10.1021/ja00282a039.

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40

Yassin, Ali, Bilal Nehmeh, Sally El Kantar, Yara Al Kazzaz, and Elias Akoury. "Synthesis of lanthanide tag and experimental studies on paramagnetically induced residual dipolar couplings." BMC Chemistry 16, no. 1 (July 21, 2022). http://dx.doi.org/10.1186/s13065-022-00847-5.

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AbstractNuclear Magnetic Resonance (NMR) spectroscopy is an indispensable technique for the structure elucidation of molecules and determination of their characteristic interactions. Residual Dipolar Coupling (RDC) is an NMR parameter that provides global orientation information of molecules but necessitates the use of an anisotropic orientation medium for the partial alignment of the target molecule with respect to the magnetic field. Importantly, anisotropic paramagnetic tags have been successful as orienting media in biomolecular NMR applications but their use in small organic molecules remains imperfect due to challenges in designing functional lanthanide complexes with varying degrees of bonding in the Ln(III) inner coordination sphere. In this study, we propose a strategy for the synthesis of the lanthanide tag 4-mercaptomethylpyridine-2,6-dicarboxylic acid, 4-MMDPA and the measurement of RDCs in a target molecule using several paramagnetic lanthanide complexes. Graphical Abstract

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41

Kretschmer, Jan, Tomáš David, Martin Dračínský, Ondřej Socha, Daniel Jirak, Martin Vít, Radek Jurok, Martin Kuchař, Ivana Císařová, and Miloslav Polasek. "Paramagnetic encoding of molecules." Nature Communications 13, no. 1 (June 8, 2022). http://dx.doi.org/10.1038/s41467-022-30811-9.

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AbstractContactless digital tags are increasingly penetrating into many areas of human activities. Digitalization of our environment requires an ever growing number of objects to be identified and tracked with machine-readable labels. Molecules offer immense potential to serve for this purpose, but our ability to write, read, and communicate molecular code with current technology remains limited. Here we show that magnetic patterns can be synthetically encoded into stable molecular scaffolds with paramagnetic lanthanide ions to write digital code into molecules and their mixtures. Owing to the directional character of magnetic susceptibility tensors, each sequence of lanthanides built into one molecule produces a unique magnetic outcome. Multiplexing of the encoded molecules provides a high number of codes that grows double-exponentially with the number of available paramagnetic ions. The codes are readable by nuclear magnetic resonance in the radiofrequency (RF) spectrum, analogously to the macroscopic technology of RF identification. A prototype molecular system capable of 16-bit (65,535 codes) encoding is presented. Future optimized systems can conceivably provide 64-bit (~10^19 codes) or higher encoding to cover the labelling needs in drug discovery, anti-counterfeiting and other areas.

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42

Goren, Elad, Liat Avram, and Amnon Bar-Shir. "Versatile non-luminescent color palette based on guest exchange dynamics in paramagnetic cavitands." Nature Communications 12, no. 1 (May 24, 2021). http://dx.doi.org/10.1038/s41467-021-23179-9.

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AbstractMulticolor luminescent portrayal of complexed arrays is indispensable for many aspects of science and technology. Nevertheless, challenges such as inaccessible readouts from opaque objects, a limited visible-light spectrum and restricted spectral resolution call for alternative approaches for multicolor representation. Here, we present a strategy for spatial COlor Display by Exploiting Host-guest Dynamics (CODE-HD), comprising a paramagnetic cavitand library and various guests. First, a set of lanthanide-cradled α-cyclodextrins (Ln-CDs) is designed to induce pseudo-contact shifts in the 19F-NMR spectrum of Ln-CD-bound guest. Then, capitalizing on reversible host-guest binding dynamics and using magnetization-transfer 19F-MRI, pseudo-colored maps of complexed arrays are acquired and applied in molecular-steganography scenarios, showing CODE-HD’s ability to generate versatile outputs for information encoding. By exploiting the widely shifted resonances induced by Ln-CDs, the guest versatility and supramolecular systems' reversibility, CODE-HD provides a switchable, polychromatic palette, as an advanced strategy for light-free, multicolor-mapping.

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