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  1. Article ; Online: Gadolinium-based Contrast Agent Biodistribution and Speciation in Rats.

    Le Fur, Mariane / Moon, Brianna F / Zhou, Iris Y / Zygmont, Samantha / Boice, Avery / Rotile, Nicholas J / Ay, Ilknur / Pantazopoulos, Pamela / Feldman, Adam S / Rosales, Ivy A / How, Ira Doressa Anne L / Izquierdo-Garcia, David / Hariri, Lida P / Astashkin, Andrei V / Jackson, Brian P / Caravan, Peter

    Radiology

    2023  Volume 309, Issue 1, Page(s) e230984

    Abstract: Background Gadolinium retention has been observed in organs of patients with normal renal function; however, the biodistribution and speciation of residual gadolinium is not well understood. Purpose To compare the pharmacokinetics, distribution, and ... ...

    Abstract Background Gadolinium retention has been observed in organs of patients with normal renal function; however, the biodistribution and speciation of residual gadolinium is not well understood. Purpose To compare the pharmacokinetics, distribution, and speciation of four gadolinium-based contrast agents (GBCAs) in healthy rats using MRI, mass spectrometry, elemental imaging, and electron paramagnetic resonance (EPR) spectroscopy. Materials and Methods In this prospective animal study performed between November 2021 and September 2022, 32 rats received a dose of gadoterate, gadoteridol, gadobutrol, or gadobenate (2.0 mmol/kg) for 10 consecutive days. GBCA-naive rats were used as controls. Three-dimensional T1-weighted ultrashort echo time images and R2* maps of the kidneys were acquired at 3, 17, 34, and 52 days after injection. At 17 and 52 days after injection, gadolinium concentrations in 23 organ, tissue, and fluid specimens were measured with mass spectrometry; gadolinium distribution in the kidneys was evaluated using elemental imaging; and gadolinium speciation in the kidney cortex was assessed using EPR spectroscopy. Data were assessed with analysis of variance, Kruskal-Wallis test, analysis of response profiles, and Pearson correlation analysis. Results For all GBCAs, the kidney cortex exhibited higher gadolinium retention at 17 days after injection than all other specimens tested (mean range, 350-1720 nmol/g vs 0.40-401 nmol/g;
    MeSH term(s) Rats ; Humans ; Animals ; Contrast Media ; Gadolinium/pharmacokinetics ; Tissue Distribution ; Prospective Studies ; Brain ; Organometallic Compounds ; Gadolinium DTPA ; Magnetic Resonance Imaging/methods
    Chemical Substances Contrast Media ; gadoteridol (0199MV609F) ; Gadolinium (AU0V1LM3JT) ; Organometallic Compounds ; Gadolinium DTPA (K2I13DR72L)
    Language English
    Publishing date 2023-11-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80324-8
    ISSN 1527-1315 ; 0033-8419
    ISSN (online) 1527-1315
    ISSN 0033-8419
    DOI 10.1148/radiol.230984
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Preparation of SNS Cobalt(II) Pincer Model Complexes of Liver Alcohol Dehydrogenase.

    Miecznikowski, John R / Jasinski, Jerry P / Kaur, Manpreet / Bonitatibus, Sheila C / Almanza, Emilse M / Kharbouch, Rami M / Zygmont, Samantha E / Landy, Kendra R

    Journal of visualized experiments : JoVE

    2020  , Issue 157

    Abstract: Chemical model complexes are prepared to represent the active site of an enzyme. In this protocol, a family of tridentate pincer ligand precursors (each possessing two sulfur and one nitrogen donor atom functionalities (SNS) and based on bis-imidazole or ...

    Abstract Chemical model complexes are prepared to represent the active site of an enzyme. In this protocol, a family of tridentate pincer ligand precursors (each possessing two sulfur and one nitrogen donor atom functionalities (SNS) and based on bis-imidazole or bis-triazole compounds) are metallated with CoCl2·6H2O to afford tridentate SNS pincer cobalt(II) complexes. Preparation of the cobalt(II) model complexes for liver alcohol dehydrogenase is facile. Based on a quick color change upon adding the CoCl2·6H2O to acetonitrile solution that contains the ligand precursor, the complex forms rapidly. Formation of the metal complex is complete after allowing the solution to reflux overnight. These cobalt(II) complexes serve as models for the zinc active site in liver alcohol dehydrogenase (LADH). The complexes are characterized using single crystal X-ray diffraction, electrospray mass spectrometry, ultra-violet visible spectroscopy, and elemental analysis. To accurately determine the structure of the complex, its single crystal structure must be determined. Single crystals of the complexes that are suitable for X-ray diffraction are then grown via slow vapor diffusion of diethyl ether into an acetonitrile solution that contains the cobalt(II) complex. For high quality crystals, recrystallization typically takes place over a 1 week period, or longer. The method can be applied to the preparation of other model coordination complexes and can be used in undergraduate teaching laboratories. Finally, it is believed that others may find this recrystallization method to obtain single crystals beneficial to their research.
    MeSH term(s) Alcohol Dehydrogenase/chemistry ; Cobalt/chemistry ; Coordination Complexes/chemistry ; Crystallography, X-Ray ; Imidazoles ; Ligands ; Liver/enzymology ; Models, Chemical ; Nitrogen/chemistry ; Spectrometry, Mass, Electrospray Ionization ; Sulfur/chemistry ; Zinc/chemistry
    Chemical Substances Coordination Complexes ; Imidazoles ; Ligands ; Cobalt (3G0H8C9362) ; Sulfur (70FD1KFU70) ; imidazole (7GBN705NH1) ; Alcohol Dehydrogenase (EC 1.1.1.1) ; cobaltous chloride (EVS87XF13W) ; Zinc (J41CSQ7QDS) ; Nitrogen (N762921K75)
    Language English
    Publishing date 2020-03-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Video-Audio Media
    ZDB-ID 2259946-0
    ISSN 1940-087X ; 1940-087X
    ISSN (online) 1940-087X
    ISSN 1940-087X
    DOI 10.3791/60668
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Preparation of sns cobalt(ii) pincer model complexes of liver alcohol dehydrogenase

    Miecznikowski, John R / Jasinski, Jerry P / Kaur, Manpreet / Bonitatibus, Sheila C / Almanza, Emilse M / Kharbouch, Rami M / Zygmont, Samantha E / Landy, Kendra R

    Journal of visualized experiments. 2020 Mar. 19, , no. 157

    2020  

    Abstract: Chemical model complexes are prepared to represent the active site of an enzyme. In this protocol, a family of tridentate pincer ligand precursors (each possessing two sulfur and one nitrogen donor atom functionalities (SNS) and based on bis-imidazole or ...

    Abstract Chemical model complexes are prepared to represent the active site of an enzyme. In this protocol, a family of tridentate pincer ligand precursors (each possessing two sulfur and one nitrogen donor atom functionalities (SNS) and based on bis-imidazole or bis-triazole compounds) are metallated with CoCl2·6H2O to afford tridentate SNS pincer cobalt(II) complexes. Preparation of the cobalt(II) model complexes for liver alcohol dehydrogenase is facile. Based on a quick color change upon adding the CoCl2·6H2O to acetonitrile solution that contains the ligand precursor, the complex forms rapidly. Formation of the metal complex is complete after allowing the solution to reflux overnight. These cobalt(II) complexes serve as models for the zinc active site in liver alcohol dehydrogenase (LADH). The complexes are characterized using single crystal X-ray diffraction, electrospray mass spectrometry, ultra-violet visible spectroscopy, and elemental analysis. To accurately determine the structure of the complex, its single crystal structure must be determined. Single crystals of the complexes that are suitable for X-ray diffraction are then grown via slow vapor diffusion of diethyl ether into an acetonitrile solution that contains the cobalt(II) complex. For high quality crystals, recrystallization typically takes place over a 1 week period, or longer. The method can be applied to the preparation of other model coordination complexes and can be used in undergraduate teaching laboratories. Finally, it is believed that others may find this recrystallization method to obtain single crystals beneficial to their research.
    Keywords X-ray diffraction ; acetonitrile ; active sites ; alcohol dehydrogenase ; cobalt ; color ; crystal structure ; crystallization ; crystals ; ethyl ether ; ligands ; liver ; mass spectrometry ; models ; nitrogen ; sulfur ; triazoles ; ultraviolet-visible spectroscopy ; vapors ; zinc
    Language English
    Dates of publication 2020-0319
    Size p. e60668.
    Publishing place Journal of Visualized Experiments
    Document type Article
    ZDB-ID 2259946-0
    ISSN 1940-087X
    ISSN 1940-087X
    DOI 10.3791/60668
    Database NAL-Catalogue (AGRICOLA)

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  4. Article: Tailored chemical reactivity probes for systemic imaging of aldehydes in fibroproliferative diseases.

    Ma, Hua / Zhou, Iris Y / Chen, Y Iris / Rotile, Nicholas J / Ay, Ilknur / Akam, Eman / Wang, Huan / Knipe, Rachel / Hariri, Lida P / Zhang, Caiyuan / Drummond, Matthew / Pantazopoulos, Pamela / Moon, Brianna F / Boice, Avery T / Zygmont, Samantha E / Weigand-Whittier, Jonah / Sojoodi, Mozhdeh / Gonzalez-Villalobos, Romer A / Hansen, Michael K /
    Tanabe, Kenneth K / Caravan, Peter

    bioRxiv : the preprint server for biology

    2023  

    Abstract: During fibroproliferation, protein-associated extracellular aldehydes are formed by the oxidation of lysine residues on extracellular matrix proteins to form the aldehyde allysine. Here we report three Mn(II)-based, small molecule magnetic resonance (MR) ...

    Abstract During fibroproliferation, protein-associated extracellular aldehydes are formed by the oxidation of lysine residues on extracellular matrix proteins to form the aldehyde allysine. Here we report three Mn(II)-based, small molecule magnetic resonance (MR) probes that contain α-effect nucleophiles to target allysine in vivo and report on tissue fibrogenesis. We used a rational design approach to develop turn-on probes with a 4-fold increase in relaxivity upon targeting. The effects of aldehyde condensation rate and hydrolysis kinetics on the performance of the probes to detect tissue fibrogenesis noninvasively in mouse models were evaluated by a systemic aldehyde tracking approach. We showed that for highly reversible ligations, off-rate was a stronger predictor of in vivo efficiency, enabling histologically validated, three-dimensional characterization of pulmonary fibrogenesis throughout the entire lung. The exclusive renal elimination of these probes allowed for rapid imaging of liver fibrosis. Reducing the hydrolysis rate by forming an oxime bond with allysine enabled delayed phase imaging of kidney fibrogenesis. The imaging efficacy of these probes, coupled with their rapid and complete elimination from the body, make them strong candidates for clinical translation.
    Language English
    Publishing date 2023-04-21
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.04.20.537707
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Tailored Chemical Reactivity Probes for Systemic Imaging of Aldehydes in Fibroproliferative Diseases.

    Ma, Hua / Zhou, Iris Y / Chen, Y Iris / Rotile, Nicholas J / Ay, Ilknur / Akam, Eman A / Wang, Huan / Knipe, Rachel S / Hariri, Lida P / Zhang, Caiyuan / Drummond, Matthew / Pantazopoulos, Pamela / Moon, Brianna F / Boice, Avery T / Zygmont, Samantha E / Weigand-Whittier, Jonah / Sojoodi, Mozhdeh / Gonzalez-Villalobos, Romer A / Hansen, Michael K /
    Tanabe, Kenneth K / Caravan, Peter

    Journal of the American Chemical Society

    2023  Volume 145, Issue 38, Page(s) 20825–20836

    Abstract: During fibroproliferation, protein-associated extracellular aldehydes are formed by the oxidation of lysine residues on extracellular matrix proteins to form the aldehyde allysine. Here we report three Mn(II)-based, small-molecule magnetic resonance ... ...

    Abstract During fibroproliferation, protein-associated extracellular aldehydes are formed by the oxidation of lysine residues on extracellular matrix proteins to form the aldehyde allysine. Here we report three Mn(II)-based, small-molecule magnetic resonance probes that contain α-effect nucleophiles to target allysine in vivo and report on tissue fibrogenesis. We used a rational design approach to develop turn-on probes with a 4-fold increase in relaxivity upon targeting. The effects of aldehyde condensation rate and hydrolysis kinetics on the performance of the probes to detect tissue fibrogenesis non-invasively in mouse models were evaluated by a systemic aldehyde tracking approach. We showed that, for highly reversible ligations, off-rate was a stronger predictor of in vivo efficiency, enabling histologically validated, three-dimensional characterization of pulmonary fibrogenesis throughout the entire lung. The exclusive renal elimination of these probes allowed for rapid imaging of liver fibrosis. Reducing the hydrolysis rate by forming an oxime bond with allysine enabled delayed phase imaging of kidney fibrogenesis. The imaging efficacy of these probes, coupled with their rapid and complete elimination from the body, makes them strong candidates for clinical translation.
    MeSH term(s) Mice ; Animals ; Aldehydes ; 2-Aminoadipic Acid/chemistry ; Magnetic Resonance Imaging ; Lung
    Chemical Substances allysine (425I4Y24YZ) ; Aldehydes ; 2-Aminoadipic Acid (1K7B1OED4N)
    Language English
    Publishing date 2023-08-17
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.3c04964
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

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